The 56th ENC
Experimental Nuclear Magnetic Resonance Conference
April 19 – 24, 2015
Asilomar Conference Grounds
Executive Committee
Dear ENC Friends
Chair
Teresa Carlomagno
Welcome back to Asilomar! It is a great pleasure and honor for me to chair the 56th ENC in
this extraordinary location where so many of us have had memorable experiences in previous
years. For those who are attending the ENC for the first time:
you will love it!
EMBL Heidelberg
Treasurer
Song-i Han
UC Santa Barbara
Secretary
M. Albert Thomas
Univ. of California, Los Angeles
Chair-Elect
Chad Rienstra
University of Illinois
Past Chair
Tatyana Polenova
University of Delaware
Rafael Bruschweiler
Ohio State University
Thomas (Adrian) Carpenter
University of Cambridge
Brad Chmelka
Univ. of California, Santa Barbara
Frank Delaglio
NMR Science
Sophia Hayes
Washington University St Louis
Jeffrey Hoch
Univ. of Connecticut Health Ctr.
Wolfgang Jahnke
Novartis Inst. for Biomedical Res.
Anne Lesage
University of Lyon
J. Patrick Loria
Yale University
Jeffrey Reimer
Univ. of California, Berkeley
Melanie Rosay
Bruker-Biospin
Ichio Shimada
University of Tokyo
Daniel B. Vigneron
Univ. of California, San Francisco
Yulan Wang
Wuhan Inst. of Physics &
Mathematics
Conference Managers
Judith Sjoberg
Jennifer Watson
Cindi Pettit
The ENC is a special conference with its own unique
atmosphere. The combination of vibrant science, a
gorgeous setting and fun evenings at the hospitality suites
creates the perfect atmosphere for scientific inspiration and
exchange of ideas. The program reflects the multi-faceted
nature of our field: in 97 oral presentations you will hear
about the most recent methodological developments and
challenging applications in solution- and solid-state NMR as
well as MRI. This year considerable space is dedicated to
dynamic nuclear polarization, which has been gaining ever
more momentum since the hardware became readily
available. In addition, three outstanding tutorial speakers will provide overviews of special
topics in the fields of theory, hardware and applications of nuclear magnetic resonance.
Equally as important as the oral presentations are the posters. I am very happy to say that this
year we have received a record number of 516 submissions. With 484 poster presentations
we are almost at the limits of capacity.
The after-dinner lecture on Thursday evening will deviate slightly from the ENC tradition.
Instead of taking us back to the old days of magnetic resonance spectroscopy, this year's
speaker will keep us more in the present while also looking forward to what the future might
hold. Gerhard Wagner, a leading scientist in biomolecular NMR, will demonstrate the
enormous potential of combining advanced technology with exciting applications. We are
looking forward to learn "where the cool things are" and how we can reach for them!
As in previous years, the ENC will distribute a number of prizes, recognizing outstanding
contributions of both early-career and established scientists. On Monday morning, Bob Griffin,
the new chair of the Laukien Prize Committee, will introduce this year's laureate. During the
after-dinner program, Lucio Frydman (Editor-in-Chief of the Journal of Magnetic Resonance)
will present the JMR Young Investigator Awards to the contributors of the three best
abstracts. Finally, the Ritchey Travel Award, established in memory of Bill Ritchey, who
founded the ENC 56 years ago, will be presented to the most deserving student on Thursday
evening.
I would also like to draw your attention to an extraordinary session chaired by Chad Rienstra
on Tuesday evening, in which ex-Varian and Agilent customers will discuss issues related to
the maintenance, update and repair of Varian and Agilent spectrometers after Agilent sadly
withdrew from the NMR business in October 2014.
Lastly, I would like to thank our sponsors, as well as the 37 corporate partners, for supporting
the ENC and for taking such good care of us in the evenings: the ENC would not be the same
without your contribution.
I wish you all great science and an unforgettable time in Asilomar!
Teresa Carlomagno
Chair, 56th ENC
See Table of Contents page 4.
Page 1
Page 2
Page 3
The 56th ENC
Experimental Nuclear Magnetic Resonance Conference
April 19 – 24, 2015
Asilomar Conference Grounds
Executive Committee
Chair
Teresa Carlomagno
TABLE OF CONTENTS
EMBL Heidelberg
Treasurer
Song-i Han
UC Santa Barbara
Secretary
M. Albert Thomas
General Information ........................................... 5
Awards .............................................................. 6
Other Awards .................................................... 8
Corporate Sponsors ........................................ 10
Univ. of California, Los Angeles
Chair-Elect
Chad Rienstra
University of Illinois
Media Partners ................................................ 11
Hospitality Suites/Exhibitors ............................ 12
Grounds Map ................................................... 13
Past Chair
Tatyana Polenova
Program Overview ........................................... 15
University of Delaware
Sunday/Monday Program ................................ 16
Rafael Bruschweiler
Ohio State University
Thomas (Adrian) Carpenter
University of Cambridge
Brad Chmelka
Univ. of California, Santa Barbara
Frank Delaglio
NMR Science
Sophia Hayes
Tuesday Program ............................................ 18
Wednesday Program ....................................... 21
Thursday Program ........................................... 23
Friday Program ................................................ 27
Abstracts of Talks ............................................ 29
Poster Program & Abstracts of Posters ........... 47
Washington University St Louis
Index of Authors ............................................ 129
Jeffrey Hoch
Directory of Participants ................................ 142
Univ. of Connecticut Health Ctr.
Wolfgang Jahnke
Novartis Inst. for Biomedical Res.
Anne Lesage
University of Lyon
J. Patrick Loria
Yale University
Jeffrey Reimer
Univ. of California, Berkeley
Melanie Rosay
Bruker-Biospin
Ichio Shimada
University of Tokyo
Daniel B. Vigneron
Univ. of California, San Francisco
Yulan Wang
Wuhan Inst. of Physics &
Mathematics
Conference Managers
Judith Sjoberg
Jennifer Watson
Cindi Pettit
Page 4
Memorial........................................................ 159
GENERAL INFORMATION
PROGRAM. The short abstracts for the talks and posters
appear in this book and are arranged in the order of
presentation. The author index references the program code
of presentations. PDF versions of long abstracts may be
viewed online: www.enc-conference.org.
POSTERS. Posters are located in the Fireside Pavilion
(underground garage). Please use stairway entrance from
Fireside Patio. All posters should be set up by 8:30 AM on
Monday and removed at 4:00 PM on Thursday. Please place
posters in the space number printed in this program. See
page 46.
•
Monday, 2:00 – 3:45 PM: Authors of posters in odd
numbered spaces (001, 003, 005, etc) present.
•
Tuesday, 2:00 – 3:45 PM: Authors of posters in even
numbered spaces (002, 004, 006 etc) present.
•
Wednesday, 2:00 – 3:45 PM: Authors of posters in odd
numbered spaces (001, 003, 005, etc) present.
•
Thursday, 2:00 – 3:35 PM: Authors of posters in even
numbered spaces (002, 004, 006, etc) present.
Posters of short talks are described on pages 127-128.
TALKS. Plenary session talks are in Merrill Hall with
overflow seating in the Chapel. Parallel session talks are
scheduled in either Merrill Hall or Chapel as indicated in the
program. Each session room has one screen and one
computer projector. Speakers are asked to use the computer
mouse as a pointer.
Speakers must appear ½ hour prior to the start of their
sessions. Speakers will use this time to connect laptops and
assure compatibility with the projector.
SHUTTLE VANS. Vans run between Asilomar and the
motels along Lighthouse Avenue according to the following
schedule:
Sunday: 3:00 PM – 11:30 PM
Monday, Tuesday, Wednesday, and Thursday
7:00-9:00 AM; noon - 2:00 PM; 5:00–11:30 PM
Friday: 7:00 - 9:00 AM; noon - 2:00 PM
AIRPORT TRANSPORTATION.
•
Call 24 hours in advance to reserve Monterey Airbus for
transportation to San Francisco or San Jose airports.
www.montereyairbus.com or call 831-373-7777.
•
To order a taxi, inquire at the Asilomar front desk.
FRIDAY BOX LUNCHES. If you are lodging at Asilomar
and would like to take a box lunch with you on Friday, please
order by Tuesday at conference registration in Triton Room.
INTERNET ACCESS. ENC has enhanced the Asilomar
WiFi in the Fireside Pavilion (poster garage) and the deck of
Surf & Sand.
HOSPITALITY SUITES & EXHIBIT BOOTHS. Vendor
hospitality suites are located throughout the Asilomar
grounds.
Exhibit booths are in the Fireside Pavilion
(underground garage) across Asilomar Blvd from the main
Asilomar entrance. Refer to page 12 for locations.
VENDOR RAFFLE. Return completed form by 12 noon on
Thursday to enter. Prize winners will be drawn at the After
Dinner Program on Thursday evening. You must be present to
win.
REGULATIONS
• Name badges are required for all conference sessions,
including the posters. A white (full registration) badge is
required for entrance to oral and poster sessions. Green
badges provide grounds access and admission to the
opening reception and hospitality suites.
• NO SMOKING is permitted in any conference area.
• Cell phones must be turned off in oral sessions.
• NO photography or recording in any session, including
posters.
• There may be no organized activities (even off-site)
other than those approved by ENC during the conference
week (5:00 PM on Sunday through noon on Friday).
SPECIAL EVENTS
Sunday, 4:00 - 6:00 PM
Reception, Merrill Hall All registrants are invited to enjoy
a tasting of artesian cheeses. No extra ticket is required,
only your ENC name badge (any color). Please present
the drink ticket in your registration envelope for wine or
beer.
Regular Asilomar dinner will be served at 6:00 pm for those
staying on-site.
Thursday, 6:30 - 8:00 PM
Conference Dinner, Crocker Hall. The dinner features an
Italian buffet and central coast wines. Tickets may be
purchased until 12 noon on Monday. Cost is $20 for onsite lodgers, $35 off-site.
Regular dinner service will be offered for those lodging at
Asilomar but who have not purchased tickets for conference
dinner.
Thursday, 8:00 – 9:00 PM
After Dinner Program, Merrill
Hall. Everyone is invited – no
ticket is needed.
Gerhard Wagner, Harvard
University Medical School
Winning the Lottery . . .
or Where the Cool Things
Are
After dinner program also
features:
• Award presentations
• Raffle of valuable prizes
EMPLOYMENT CENTER. Poster boards in the Triton
Room are provided for employment notices. If you are
seeking employment, please supply at least 20 copies of your
résumé to the Triton Room after 10:00 AM on Monday. The
résumés will be filed for public perusal.
Page 5
GÜNTHER LAUKIEN PRIZE 2015
The 2015 Günther Laukien Prize is awarded to Professor Arthur G. Palmer III for
his innovative and elegant solution NMR studies of protein dynamics and
thermodynamics, and for his seminal contributions to elucidating molecular motions
on time scales that span several orders of magnitude. His many ingenious
experiments have extended the reach of NMR beyond static three-dimensional
structural studies, enabling detailed insight into biomolecular function. He has
further enhanced the capabilities of the solution NMR community by developing and
disseminating robust software that is widely used for analyzing spin relaxation data
of proteins.
Art received a B.A. in chemistry magna cum laude in 1980 from Haverford College.
There he conducted undergraduate research in the photochemistry of carbonyl
carbene with Prof. Colin F. Mackay. After two years working as an analytical
chemist and two years teaching high school chemistry and physics, Palmer entered
graduate school, first receiving an M.S. in Industrial Health from the University of
Michigan in 1986 and the Ph.D. from the University of North Carolina at Chapel Hill
in 1989. His doctoral research, conducted under the direction of Prof. Nancy L.
Thompson, developed the technique of high order autocorrelation in fluorescence
correlation spectroscopy. Palmer made the jump to NMR spectroscopy as a
National Science Foundation Postdoctoral Fellow with Dr. Peter E. Wright at the
Scripps Research Institute from 1989-1992. There Palmer co-developed, with
Wright, Mark Rance, and John Cavanagh, the sensitivity-enhanced HSQC and
related experiments and began his first developments and applications of NMR spin
relaxation to characterize macromolecular dynamics. Palmer moved to the
Department of Biochemistry and Molecular Biophysics at Columbia University as an Assistant Professor in 1992; he was
promoted to Associate Professor with tenure in 1998 and to Professor in 2001. He currently holds the Robert Wood Johnson Jr.
Chair and serves as Vice Chair of the Department of Biochemistry and Molecular Biophysics and as Associate Dean for
Graduate Affairs at Columbia University Medical Center. He also is the Director of NMR Spectroscopy at the New York
nd
Structural Biology Center and served as Chair of the 42 ENC.
Palmer is the author of 134 papers and the co-author, with John Cavanagh, Wayne J. Fairbrother, Nicholas J. Skelton, and Mark
Rance, of the book “Protein NMR Spectroscopy: Principles and Practice”, now in its second edition. He also is the author of the
program ModelFree, which is widely used for analysis of spin relaxation data using the Lipari-Szabo model-free formalism.
Palmer uses NMR spectroscopy and molecular dynamics simulations to elucidate the coupling between conformational
dynamical properties and biological functions of proteins. His research interests include development of novel methods in NMR
spectroscopy, computational and theoretical analyses of protein dynamics, and applications to protein folding, molecular
recognition, and catalysis. He has contributed in particular to the use of generalized order parameters for characterizing
conformational entropic effects in molecular recognition, and the use of CPMG and R1 relaxation dispersion measurements for
characterizing microsecond-millisecond time scale processes. Recently, he has used molecular dynamics simulations to aid in
interpretation of NMR spin relaxation measurements. Palmer has long been interested in the conformational dynamic
differences between mesophilic and thermophilic enzymes that contribute to differences in activity, using the ribonuclease H
superfamily as a model system. Other recent applications include the mechanism of strand swapping in dimerization of cadherin
cell adhesion proteins, the role of local dynamics in DNA recognition by the GCN4 bZip transcription factor, dynamic control of
the order of substrate addition in the DNA-repair enzyme AlkB, and the mechanism of autoinhibition of the Crk-II signaling
adapter protein. A selected set of Palmer’s publications, one per year, is provided below.
• K. A. Stafford, N. Trbovic, J. A. Butterwick, R. Abel, R. A. Friesner, and A. G. Palmer, Conformational preferences underlying reduced activity
of a thermophilic ribonuclease H, J. Mol. Biol., in press (2015). doi:10.1016/j.jmb.2014.11.023.
• M. L. Gill and A. G. Palmer, Local isotropic diffusion approximation for coupled internal and overall molecular motions in NMR spin relaxation,
J. Phys. Chem. B 118, 11120-11128 (2014). doi: 10.1021/jp506580c. PMCID: PMC4174990.
• Y. Li, N. Altorelli, F. Bahna, B. Honig, L. Shapiro and A. G. Palmer, Mechanism of E-cadherin dimerization probed by NMR relaxation
dispersion, Proc. Nat. Acad. Sci. USA 110, 16462–16467 (2013). doi: 10.1073/pnas.1314303110. PMCID: PMC3799306.
• P. Robustelli, K. A. Stafford, and A. G. Palmer, Interpreting protein structural dynamics from NMR chemical shifts, J. Am. Chem. Soc. 134,
6365–6374 (2012). doi: 10.1021/ja300265w. PMCID: PMC3324661.
• J.-H. Cho, V. Muralidharan, M. Vila-Perello, D. P. Raleigh, T. W. Muir, and A. G. Palmer, Tuning protein autoinhibition by domain
destablization, Nat. Struct. Mol. Biol. 18, 550-555 (2011). doi:10.1038/nsmb.2039. PMCID: PMC3265570.
• Y. Li and A. G. Palmer, Narrowing of protein NMR spectral lines broadened by chemical exchange, J. Am. Chem. Soc. 132, 8856-8857
(2010). PMCID: PMC2921271.
• N. Trbovic, J. Cho, R. Abel, R. A. Friesner, M. Rance, and A. G. Palmer, Protein side-chain dynamics and residual conformational entropy, J.
Am. Chem. Soc. 131, 615–622 (2009). PMCID: PMC2413295.
• P. Maragakis, K. Lindorff-Larsen, M. P. Eastwood, R. O. Dror, J. L. Klepeis, I. T. Arkin, M. Ø. Jensen, H. Xu, N. Trbovic, R. A. Friesner, A. G.
Palmer, and D. E. Shaw, Microsecond molecular dynamics simulation shows effect of slow loop dynamics on backbone amide order
parameters of proteins, J. Phys. Chem. B 112, 6155-6158 (2008). PMCID: PMC2805408.
• T. I. Igumenova, U. Brath, M. Akke, and A. G. Palmer, Characterization of chemical exchange using residual dipolar coupling, J. Am. Chem.
Soc. 129, 13396-13397 (2007). PMCID: PMC2527592.
Page 6
AWARDS
Arthur G. Palmer, continued
• M. J. Grey, Y. Tang, E. Alexov, C. J. McKnight, D. P. Raleigh, and A. G. Palmer, Characterizing a partially folded intermediate of the villin
headpiece domain under non-denaturing conditions: Contribution of His41 to the pH-dependent stability of the N-terminal subdomain, J. Mol.
Biol. 355, 1078-1094 (2006).
• F. Massi, M. J. Grey, and A. G. Palmer, Microsecond time-scale backbone conformational dynamics in ubiquitin studied with NMR R1 
relaxation experiments, Protein Sci. 14, 735-742 (2005).
• F. Massi, E. Johnson, C. Wang, M. Rance, and A. G. Palmer, NMR R1 rotating-frame relaxation with weak radiofrequency fields, J. Am.
Chem. Soc. 126, 2247-2256 (2004).
• M. J. Grey, C. Wang, and A. G. Palmer, Disulfide bond isomerization in basic pancreatic trypsin inhibitor: Multi-site chemical exchange
quantified by CPMG relaxation dispersion and chemical shift modeling, J. Am. Chem. Soc. 125, 14324-14335 (2003).
• O. Trott and A. G. Palmer, R1 relaxation outside of the fast-exchange limit, J. Magn. Reson. 154, 157-160 (2002).
• G. Palmer, C. D. Kroenke, and J. P. Loria, NMR methods for quantifying microsecond-to-millisecond motions in biological macromolecules,
Meth. Enzymol. 339, 204-238 (2001).
• O. Millet, J. P. Loria, C. D. Kroenke, M. Pons, and A. G. Palmer, The static magnetic field dependence of chemical exchange linebroadening
defines the NMR chemical shift time scale, J. Am. Chem. Soc. 122, 2867-2877 (2000).
• J. P. Loria, M. Rance, and A. G. Palmer, A relaxation-compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical
exchange by NMR spectroscopy, J. Am. Chem. Soc. 121, 2331-2332 (1999).
• C.D. Kroenke, J.P. Loria, L.K. Lee, M. Rance, and A.G. Palmer, Longitudinal and transverse 1H-15N dipolar/15N chemical shift anisotropy
relaxation interference: Unambiguous determination of rotational diffusion tensors and chemical exchange effects in biological
macromolecules, J. Am. Chem. Soc. 120, 7905-7915 (1998).
• L. K. Lee, M. Rance, W. J. Chazin and A. G. Palmer, Rotational diffusion anisotropy of proteins from simultaneous analysis of 15N and 13C
nuclear spin relaxation, J. Biomol. NMR 9, 287-298 (1997).
• M. Akke and A. G. Palmer, Monitoring macromolecular motions on microsecond-millisecond time scales by R1 -R1 constant relaxation time
NMR spectroscopy, J. Am. Chem. Soc. 118, 911-912 (1996).
• M. Mandel, M. Akke and A. G. Palmer, Backbone dynamics of Escherichia coli ribonuclease HI: Correlations with structure and function in an
active enzyme, J. Mol. Biol. 246, 144-163 (1995).
• M. Mandel and A. G. Palmer, Measurement of relaxation rate constants using constant-time, accordion, heteronuclear NMR spectroscopy, J.
Magn. Reson., Ser. A 110, 62-72 (1994).
• M. Akke, R. Brüschweiler and A. G. Palmer, NMR order parameters and free energy: An analytical approach and application to cooperative
Ca2+ binding by calbindin D9k, J. Am. Chem. Soc. 115, 9832-9833 (1993).
• G. Palmer, N. J. Skelton, W. J. Chazin, P. E. Wright and M. Rance, Suppression of the effects of cross-correlation between dipolar and
anisotropic chemical shift relaxation mechanisms in the measurement of spin-spin relaxation rates, Molec. Phys. 75, 699-711 (1992).
• G. Palmer, M. Rance and P. E. Wright, Intramolecular motions of a zinc finger DNA-binding domain from Xfin characterized by protondetected natural abundance 13C heteronuclear NMR spectroscopy, J. Am. Chem. Soc. 113, 4371-4380 (1991).
• G. Palmer and N. L. Thompson, High order fluorescence fluctuation analysis of model protein clusters, Proc. Natl. Acad. Sci. U.S.A. 86, 61486152 (1989).
• L. L. Wright, A. G. Palmer and N. L. Thompson, Inhomogeneous translational diffusion of monoclonal antibodies on phospholipid LangmuirBlodgett films, Biophys. J. 54, 463-470 (1988).
• G. Palmer and N. L. Thompson, Molecular aggregation characterized by high order autocorrelation in fluorescence correlation spectroscopy,
Biophys. J. 52, 257-270 (1987).
2016 GÜNTHER LAUKIEN PRIZE:
CALL FOR NOMINATIONS
The Laukien Prize was established in 1999 to honor the memory of Professor Günther Laukien, a co-founder of Bruker. The
Laukien Prize carries a monetary award of $20,000 funded by Bruker and is intended to recognize cutting-edge experimental
NMR research with a high probability of enabling beneficial new applications. The Prize recipient will also deliver the opening
Plenary lecture at the ENC conference.
The deadline for nominations is October 31. The award is announced at the annual ENC. The nominated work should be
published within the last three years. In some special cases, the award may be for cumulative achievements over a longer
period.
Nominations should include:
1. Name of nominee, the nominees affiliation, address, phone, fax and e-mail.
2. Name of nominator, address, phone, fax and e-mail.
3. A brief (no more than 200 words) description of the work serving as the basis for the nomination.
4. A list of relevant publications (no more than 5).
Page 7
SURAJ P. MANRAO SCIENCE FUND
ENC is pleased to acknowledge the continuation of support from the Suraj P. Manrao Student Travel
Fund. During his long career, Mr. Manrao has been dedicated to the NMR community and has a special
interest in helping and guiding young scientists in the beginning of their careers. This fund represents
his commitment to this community and an investment in the future of young post-doctoral fellows and
graduate students.
Student Travel Recipients funded by Suraj Manrao Science Foundation
Owen Becette
Shelby Follett
Somnath Mondal
University of Maryland
University of Wyoming
Indian Institute of Science
Robert Blum
Alexander Forse
Maria Theresia Pöschko
Yale University
University of Cambridge
Johannes Kepler University
Thach Can
Steffen Goerke
Vijaykumar Ramaswamy
MIT
German Cancer Research
Center
Rivkah Rogawski
Maria Conrad Soria
University of Florida
U. of Southern California
Derrick Kaseman
Columbia University
D. Levi Craft
University of California, David
Shannon Sweeney
University of Texas at Austin
Bucknell University
Singh Kawarpal
Joshua Damron
RWTH Aachen University
Meaghan Ward
University of Michigan
N. Lokesh
University of Guelph
Jitendra Kumar Das
Indian Institute of Science
Le Zhang
CSIR - IICB
Nikita Malik
UNC Chapel Hill
Indian Inst. of Technology
Bombay
RITCHEY TRAVEL AWARD
The ENC Ritchey Travel Award is established to honor William M. Ritchey, who
founded the ENC in 1960. The award is funded with contributions from Professor
Ritchey’s former students. The areas of the Award are to reflect Prof. Ritchey’s broad
interests in the development and application of NMR to chemical and material
sciences. The amount of the annual Award is $1,000 to be used for travel to the ENC.
The 2015 recipient of the ENC Ritchey Travel Award is Laura Castañar Acedo,
Universitat Autonòma de Barcelona. Her talk “HOBS: Broadband Homonuclear
Decoupled Band-Selective NMR Experiments with Full Sensitivity” is scheduled at 12:15–12:30 PM,
Tuesday, Chapel. The award will be presented at the After-Dinner Program, 8:00 PM, Thursday in
Merrill Hall.
JMR AWARDS
Sponsored by Journal of Magnetic Resonance, Elsevier Science Publishing
The annual JMR Awards are selected from abstracts submitted by graduate students or post-doctoral fellows. Each award
includes a prize of $350 funded by Elsevier Science Publishing and a one year personal subscription to JMR. The prizes will be
presented by Editor Lucio Frydman at the After Dinner Program on Thursday at 8:00 PM, Merrill Hall.
Andrew Ilott
New York University
“The Principle of Reciprocity in
Conductors;” scheduled 12:15–12:30
PM, Wednesday, Chapel.
Page 8
Guillaume Mas
Structural Biology Institute, Grenoble
“Studies of a 1 MDa Chaperonin in
Action by Combined NMR and EM
Approaches;” scheduled 12:00-12:15
PM, Monday, Merrill Hall
Guinevere Mathies
MIT
“Efficient Dynamic Nuclear Polarization
at 800 MHz with Trityl-Nitroxide
Biradicals;” scheduled 11:50-12:05 AM,
Monday, Merrill Hall.
STUDENT TRAVEL STIPENDS
Stipends are funded by ENC and these donors
Wilmad-Lab Glass
Isotec/Sigma Aldrich
Magritek Limited

MR Resources
New Era Enterprises
Student Travel Recipients funded by the sponsors above and ENC
Adewale Akinfaderin
Fangling Ji
Adam Smith
Florida State University
DLUT
University of Florida
Thomas Bauer
Mohammed Kaplan
Reza Tavakoli Dinani
ETH Zurich
Universiteit Utrecht
Simon Fraser University
Richard Bounds
Sophie Koroloff
David Waddington
University Of Southampton
North Carolina State University
MGH/A.A. Martinos Center
Qiaoyan Chen
Tanguy Le Marchand
Brennan Walder
SIBET, CAS
ISA Université de Lyon
The Ohio State University
Ren-Hao Cheng
Chia-Ying Lee
Xiaoling Wang
Natl Sun Yat-sen Univer
National Chung Cheng University
Virginia Tech
Yong-Geun Choi
Yalda Liaghati Mobarhan
Yanfei Wang
Gyeongsang National University
University of Toronto
University of Pennsylvania
Sarah Clark
Guillermo Lucena
Xuan Wei
Oregon State University
University of Sussex
MIT
Basant Dhital
Daniele Mammoli
Matthew Willmering
CUNY Graduate Center
École polytechnique féd. de Lausanne
Washington University in STL
Samuel Einstein
Lauren Marbella
Johannes Wittmann
University of Minnesota
University of Pittsburgh
ETH Zurich
Nan Eshuis
Guillaume Mas
Bing Wu
Radboud University
Structural Biology Institute
Dublin City University
Simon Glanzer
Lauren ODonnell
Milan Zachrdla
University of Graz / Institute of Chemistry
University of Miami
Masaryk University, CEITEC
Muller Gomes
Christopher O'Keefe
Matthew Zambrello
University of California, Berkeley
University of Windsor
University of Connecticut
Leah Heist
Yusuke Okuno
Jianping Zhong
UNC Chapel Hill
University of Wisconsin-Madison
Wuhan Inst. of Physics & Math., CAS
Ryeo Yun Hwang
Alexandra Pozhidaeva
Zijian Zhou
Korea Basic Science Institute
UCONN Health Center
Duke University
Tony Reinsperger
KIT
Page 9
CORPORATE SPONSORS
ENC is pleased to acknowledge the generous support of the following companies.
Major Sponsors
Sponsors
Page 10
MEDIA PARTNERS
ENC is pleased to acknowledge the advertising support of these Publishers and Journals.
Elsevier Science
Springer-Verlag
Wiley-Blackwell
Journal of
Magnetic Resonance
Journal of
Biomolecular NMR
Magnetic Resonance in Chemistry
Progress in Nuclear Magnetic
Resonance Spectroscopy
NMR in Biomedicine
Solid State Nuclear Magnetic
Resonance
Page 11
HOSPITALITY SUITES AND EXHIBIT BOOTHS
Hospitality Suites
Exhibit Booths
Sunday
After 8:00 PM (optional)
Monday - Wednesday
After 6:00 PM
2:00 – 4:00 PM
Thursday
After 6:00 PM (optional)
2:00 – 4:00 PM
Be sure to enter the raffle by asking exhibitors to apply labels to your card at each suite and exhibit booth. Completed cards
must be returned to the conference registration in Triton by noon on Thursday for drawing on Thursday evening.
COMPANY
LOCATION
ACD / LABS
BRUKER BIOSPIN CORP
CAMBRIDGE ISOTOPE LABS
CPC
Kiln
Marlin
Willow Living Room, 1st Floor
CRYOGENIC
Exhibit booth in Fireside Pavilion
DAEDALUS INNOVATIONS LLC
Exhibit booth in Fireside Pavilion
DOTY SCIENTIFIC, INC.
Toyon
ELSEVIER SCIENCE LTD
Tabletop in Fireside Pavilion
ISOTEC/SIGMA ALDRICH
Sanderling
JEOL USA, INC
Fred Farr South
JS RESEARCH, INC.
Manzanita Living Room, 2nd Floor
KIMBLE CHASE LLC
Exhibit booth in Fireside Pavilion
MAGRITEK LIMITED
Afterglow
MESTRELAB RESEARCH
MR RESOURCES
NEW ERA ENTERPRISES
NMR ASSOCIATES
Curlew
Oak Knoll Living Room, 1st Floor
Forest Lodge 1211
Scripps Conference Room
NMR-Bio/CEA
Exhibit booth in Fireside Pavilion
NMR INSTITUTE
Exhibit booth in Fireside Pavilion
NORELL, INC
OPEN TECHNOLOGIES, INC
PhoenixNMR
PROTASIS CORP
Dolphin
Scripps Conference Room
Embers Living Room
Oak Shelter
PURE DEVICES GmbH
Exhibit booth in Fireside Pavilion
QUANTUM DESIGN, INC
Exhibit booth in Fireside Pavilion
RESONANCE CONSULTING
REVOLUTION NMR LLC
Scripps Conference Room
Embers Living Room
SHIGEMI, INC
Manzanita Living Room, 1st Floor
SILANTES GmbH
Exhibit booth in Fireside Pavilion
SP SCIENTIFIC
Exhibit booth in Fireside Pavilion
SPRINGER-VERLAG NEW YORK INC
STELAR s.r.l.
TECMAG
TOMCO TECHNOLOGIES
TRIANGLE ANALYTICAL, INC
WILEY-BLACKWELL
WILMAD - LABGLASS
Page 12
Acacia
Tabletop in Fireside Pavilion
Exhibit booth in Fireside Pavilion
Fred Farr North
Exhibit booth in Fireside Pavilion
Manzanita Living Room, 1st Floor
Poster
Hearth Living Room
ASILOMAR GROUNDS MAP
Page 13
Page 14
56th ENC PROGRAM OVERVIEW
SUNDAY
April 19
MONDAY
April 20
3:00 - 9:00 PM, Registration, Triton
4:00 - 6:00 PM, Welcome Reception, Merrill Hall
8:00 - 11:30 PM, Hospitality Suites (Optional)
8:30 - 10:15 AM, Welcome and Laukien Prize Lecture
Merrill Hall, overflow seating in Chapel
10:15 - 10:45 AM, Break
10:45 AM - 12:30 PM, (MOB) Bioliquids: Challenging Systems
Merrill Hall, overflow seating in Chapel
12:30 - 2:00 PM, Lunch Break
2:00 - 3:45 PM, Poster Session, Fireside Pavilion
4:00 – 6:00 PM, (MOD)
4:00 – 6:00 PM, (MOE)
NMR in Chemical Biology & Drug Design
Materials
Merrill Hall
Chapel
After 6:00 PM, Hospitality Suites
8:30 - 10:15 AM, (TOA) Biosolids I, Merrill Hall, overflow seating in Chapel
TUESDAY
April 21
10:15-10:45 AM, Break
10:45 - 12:30 PM, (TOB)
10:45 - 12:30 PM, (TOC)
Conformational Dynamics & Allostery
Metabolomics & Small Molecules
Merrill Hall
Chapel
12:30 - 2:00 PM, Lunch Break
2:00 - 3:45 pm, Poster Session, Fireside Pavilion
4:00 – 5:50 PM, (TOD)
4:00 - 5:50 PM, (TOE)
NMR & Computation in Structure
Novel MRI Applications
Calculation. Merrill Hall
Chapel
After 6:00 pm, Hospitality Suites
8:30 - 10:15 AM, (WOA) Electron Meets Nucleus, Merrill Hall
WEDNESDAY
April 22
10:15-10:45 AM, Break
10:45 AM - 12:30 PM, (WOB)
10:45 AM - 12:30 PM, (WOC)
Bioliquids, Merrill Hall
Exotica, Chapel
12:30 - 2:00 PM, Lunch Break
2:00 - 3:45 PM, Poster Session
4:00 – 6:00 PM, Tutorial Session, Merrill Hall
After 6:00 PM, Hospitality Suites
8:30 - 10:05 AM, (ThOA) Methods Development in MRI, Merrill Hall
THURSDAY
April 23
10:15 - 10:45 am, Break
10:45 AM - 12:35 PM, (ThOB)
10:45 AM - 12:30 PM, (ThOC)
DNP Methods & Applications
Computational NMR: Predicting Spectra &
Chemical Shifts, Chapel
Merrill Hall
12:30 - 2:00 PM, Lunch Break
2:00 - 3:45 PM, Poster Session
4:00 – 6:00 PM, (ThOD)
4:00 - 6:00 PM, (ThOE)
Biosolids II, Merrill Hall
Instrumentation, Chapel
Hospitality Suites, optional
6:30 PM, Banquet Dinner, ticket required, Crocker Dining Hall
8:00 PM, After Dinner Program, Merrill Hall
8:30 - 10:15 AM, (FOA) Dynamics: Methods & Applications, Merrill Hall
FRIDAY
April 24
10:15 - 10:45 AM, Break
10:45 AM - 12:30 PM, (FOB) The Quest for a Better Signal:
Improving Sensitivity & Resolution, Merrill Hall
Page 15
SUNDAY, APRIL 19
4:00 - 6:00 PM, MONDAY AFTERNOON
WELCOME RECEPTION, Merrill Hall
(Regular Asilomar dinner will be served in Crocker Dining Hall.)
After 8:00 PM, HOSPITALITY SUITES OPEN (optional)
MONDAY, APRIL 15
All posters should be set up Monday morning.
Be sure to use the poster space numbers with the abstracts in this program.
See page 47.
8:30 – 10:15 AM, MONDAY MORNING
Welcome
LAUKIEN SESSION
Teresa Carlomagno, presiding
Merrill Hall
th
8:30 – 8: 50
Welcome to the 56 ENC, Teresa Carlomagno
8:50 – 9:15
Presentation of the Laukien Prize, Robert Guy Griffin
9:15 – 10:15
The Laukien Lecture, Arthur G. Palmer, III
10:15 – 10:45 AM, Break
10:45 AM – 12:30 PM, MONDAY MORNING
BIOLIQUIDS: CHALLANGING SYSTEMS
Tatyana Polenova, presiding
Merrill Hall
MOB 10:45-11:10
Abstract Page
Molecular Chaperones in Action; Charalampos Babis Kalodimos; Rutgers University,
Piscataway, NJ ............................................................................................................................................. 29
MOB 11:10-11:35
NMR and EPR as a Tool to Study the Assembly and Structure of a Large Multicomponent
1, 2
1
1
1
Protein-RNA Complex; Olivier Duss ; Maxim Yulikov ; Erich Michel ; Gunnar Jeschke ;
1 1
2
Frederic H.-T. Allain ; ETH Zurich, Zurich, Switzerland; The Scripps Research Institute, La
Jolla, CA ....................................................................................................................................................... 29
MOB 11:35-12:00
Rapid and Accurate Assignment of Larger Protein Resonances with Time-Shared
Acquisition, Non-uniform Sampling, and Covariance NMR; Dominique Frueh; Subrata
Mishra; Bradley Harden; Scott Nichols; Andrew Goodrich; Johns Hopkins School of Medicine,
Baltimore, MD ............................................................................................................................................... 29
MOB 12:00-12:15
Studies of a 1 MDa Chaperonin in Action by Combined NMR and EM Approaches;
Guillaume Mas; Pavel Macek; Elodie Crublet; Christine Moriscot; Schanda Paul; Schoehn Guy;
Boisbouvier Jerome; Structural Biology Institute, Grenoble, France (also poster 470 on
Mon/Tues) .................................................................................................................................................... 29
MOB 12:15-12:30
Solution Structure of the 108 nt J-K Region from the Encephalomyocarditis Virus IRES
1
2
3
4
4
RNA; Shunsuke Imai ; Michael Durney ; Xiaobing Zuo ; Tatyana Pestova ; Christopher Hellen ;
2
1 1
2
Victoria D'Souza ; Gerhard Wagner ; Havard Medical School, Boston, MA; Harvard University,
3
4
Cambridge, MA; Argonne National Laboratory, Chicago, IL; SUNY Downstate Medical Center,
Brooklyn, NY................................................................................................................................................. 29
12:30 – 2:00 PM, Lunch Break
2:00 – 3:45 PM, MONDAY AFTERNOON
POSTER SESSION, Fireside Pavillion
Posters begin on page 47. Authors of odd number spaces (001, 003, 005, etc) present on Monday and Wednesday.
Fiesta Snacks
Page 16
MONDAY, CONTINUED
4:00 – 6:00 PM, MONDAY AFTERNOON
NMR IN CHEMICAL BIOLOGY AND DRUG DESIGN
Ichio Shimada, presiding
Merrill Hall
MOD 4:00-4:25
Abstract Page
NMR-aided Discovery of an Allosteric Bcr-Abl Inhibitor in Clinical Trials for the Treatment
of CML; Wolfgang Jahnke; Novartis Institutes for Biomedical Research, Basel, Switzerland ...................... 29
MOD 4:25-4:50
eNOE for Protein and Protein-Ligand Complex Studies; Roland Riek; Beat Voegeli; Julien
Orts; Celestine Chi; Dean Strotz; Marielle Wälti; ETH Zurich, Zurich, Switzerland....................................... 30
MOD 4:50-5:15
Membrane Interaction and Conformational Equilibrium of Nanodisc-tethered KRAS and its
1
2
1
Oncogenic Mutants; Mitsu Ikura ; Mohammad Mazhab-Jafari ; Zhenhao Feng ; Matthew J
1
1 1
2
Smith ; Christopher B Marshall ; Princess Margaret Cancer Centre, Toronto, CA; Hospital for
Sick Children, Toronto, CA ........................................................................................................................... 30
MOD 5:15-5:30
Structural and Dynamic Features of F-recruitment Site Driven Substrate Phosphorylation
1
1
1
2
by ERK2;; Andrea Piserchio ; Venkatesh Ramakrishnan ; Hsin Wang ; Tamer Kaoud ; Boris
3
4
2
1 1
Arshava ; Kaushik Dutta ; Kevin Dalby ; Ranajeet Ghose ; The City College of New York, New
2
3
York, NY; University of Texas, Austin, TX; The College of Staten Island, Staten Island, NY;
4
The New York Structural Biology Center, New York, NY ............................................................................ 30
MOD 5:30-5:45
Ligand-Protein Screening by Long-Lived States of Fluorine-19 Nuclei; Roberto Buratto ;
1
1
1, 2
1
1
Daniele Mammoli ; Aurélien Bornet ; Estel Canet ; Basile Vuichoud ; Jonas Milani ; Sami
1
1, 2 1
2
Jannin ; Geoffrey Bodenhausen ; EPFL, Lausanne, Switzerland; ENS, Paris, France (also
poster 471 on Mon/Tues) ............................................................................................................................. 30
MOD 5:45-6:00
Real-Time Monitoring of Enzymatic Reactions in Living Cells by NMR and Its Applications
in Drug Discovery; Jun Hu; AstraZeneca, Waltham, MA (also poster 472 on Mon/Tues) .......................... 30
1
4:00 – 6:00 PM, MONDAY AFTERNOON
MATERIALS
Brad Chmelka, presiding
Chapel
35
14
15
MOE 4:00-4:25
Screening of Active Pharmaceutical Ingredients via Cl, N and N Solid-State NMR;
1
1
1
1
Robert W. Schurko ; Michael Jaroszewicz ; Andrew Namespetra ; Anthony Sandre ; Marcel
1
1
1
1
2
Hildebrand ; Hiyam Hamaed ; Stanislav Veinberg ; Karen Johnston ; Lucio Frydman ; Marek
3
4
5
5 1
Pruski ; Takeshi Kobayashi ; Ivan Hung ; Zhehong Gan ; University of Windsor, Windsor,
2
3
Canada; Weizmann Institute, Rehovot, Israel; Ames Laboratory, Iowa State University, Ames,
4
5
IA; Iowa State University, Ames, IA; NHMFL, Tallahassee, FL.................................................................. 31
MOE 4:25-4:50
Applications in the Study of Technological and Cultural Materials; Cecil Dybowski ; Jaclyn
1
1
1
1
1
1
Catalano ; Anna Murphy ; Yao Yao ; Sean Holmes ; Fahri Alkan ; Shelby Chan ; Nicholas
3
2 1
2
Zumbulyadis ; Silvia Centeno ; University of Delaware, Newark, DE; The Metropolitan Museum
3
of Art, New York, NY; Independent Researcher, Rochester, NY ................................................................ 31
MOE 4:50-5:15
DNP Enhanced Solid-State NMR Spectroscopy of Materials; Lyndon Emsley ; ENS Lyon,
2
Villeurbanne, France; EPFL, Lausanne, Switzerland .................................................................................. 31
MOE 5:15-5:30
High Resolution Solid-State NMR of Highly Radioactive Materials: A new insight into the
5f-chemistry of paramagnetic compounds; Laura Martel; Chris Selfslag; Joseph Somers;
JRC-ITU, Eggenstein Leopoldshafen, Germany (also poster 473 on Mon/Tues) ......................................... 31
MOE 5:30-5:45
Dynamic Nuclear Polarization enhanced Solid State NMR of Insensitive Nuclei: Oxygen-17
at Natural Abundance and Low-gamma Yttrium-89; Frédéric Blanc; University of Liverpool,
Liverpool, UK (also poster 474 on Mon/Tues) .............................................................................................. 31
MOE 5:45-6:00
25
1
1, 2 1
1
1
Mg NMR Studies of Mg-ion Battery Materials; Hao Wang ; Danielle Proffit ; Cheon Jung
3
1
2
2
3
1
Kim ; Premkumar Senguttuvan ; Victor Duffort ; Linda Nazar ; Jordi Cabana ; Anthony Burrell ;
1
1 1
2
John Vaughey ; Baris Key ; Argonne National Laboratory, Lemont, IL; University of Waterloo,
3
Waterloo, Canada; University of Illinois at Chicago, Chicago, IL (also poster 475 on Mon/Tues) ............... 31
After 6:00 PM, HOPITALITY SUITES
Page 17
TUESDAY, APRIL 21
8:30 – 10:15 AM, TUESDAY MORNING
BIOSOLIDS I
Anne Lesage, presiding
Merrill Hall
TOA 8:30-8:55
Abstract Page
1, 2
Structure and Dynamics of HIV-1 Protein Assemblies by MAS NMR; Tatyana Polenova ;
1
1
1
1
1
Manman Lu ; Christopher Suiter ; Huilan Zhang ; Guangjin Hou ; Mingzhang Wang ; Rupal
1
1
1
3
3
2, 4
Gupta ; Caitlin Quinn ; Xingyu Lu ; Jinwoo Ahn ; In-Ja Byeon ; Angela Gronenborn ;
1
2
University of Delaware, Newark; Pittsburgh Center for HIV Protein Interactions, Pittsburgh, PA;
3
4
University of Pittsburgh School of Medicine, Pittsburgh, PA; University of Pittsburgh, Pittsburgh,
PA ................................................................................................................................................................ 32
1
1
TOA 8:55-9:20
Structural Studies of Y145Stop Prion Protein Amyloids; Theint Theint ; Philippe S. Nadaud ;
1
1
2
2
1 1
Darryl Aucoin ; Zhe Qi ; Krystyna Surewicz ; Witold K. Surewicz ; Christopher P. Jaroniec ; The
2
Ohio State University, Columbus, OH; Case Western Reserve University, Cleveland, OH ........................ 32
TOA 9:20-9:45
MAS NMR Studies of Biomaterial Interfaces Between Bone-like Apatite and Its Regulatory
1
1
1
1
Proteins and Peptides; Gil Goobes ; Irina Matlahov ; Taly Iline-Vul ; Alex Kulpanovich ;
2
1
1
1
Elizabeth M. Y. Lee ; Yasmin Geiger ; Merav Nadav-Tsubery ; Keren Keinan-Adamsky ; Jeffrey
2 1
2
Gray ; Bar Ilan University, Ramat Gan, ISRAEL; Johns Hopkins University, Baltimore, MD ..................... 32
TOA 9:45-10:00
Structure of an RNA by Solid-State NMR; Alexander Marchanka ; Bernd Simon ; Gerhard
2
1 1
2
Althoff ; Teresa Carlomagno ; EMBL, Heidelberg, Germany; Bruker BioSpin, Rheinstetten,
Germany (also poster 476 on Mon/Tues) ..................................................................................................... 32
TOA 10:00-10:15
The Capsid Model of Intact M13 Bacteriophage from MAS NMR and Rosetta Modeling: a
1
2
Quadrupled Hydrophobic Viral Packing Epitope; Omry Morag ; Nikolaos Sgourakis ; Gili
1
3
1 1
2
Abramov ; David Baker ; Amir Goldbourt ; Tel Aviv University, Tel Aviv, Israel; NIDDK, NIH,
3
Bethesda, MR; University of Washington, Seattle, WA (also poster 477 on Mon/Tues) ............................. 32
1
10:15 – 10:45 AM
Break
Page 18
1
TUESDAY, continued
10:45 AM – 12:30 PM, TUESDAY MORNING
CONFORMATIONAL DYNAMICS AND ALLOSTERY
Patrick Loria, presiding
Merrill Hall
TOB 10:45-11:10
Abstract Page
Investigating the Role of Protein Mobility in Interdomain Communication; Xingsheng
1
1
2
1
3
4
Wang ; Jill Bouchard ; Junchao Xia ; Brendan Mahoney ; John S. Zintsmaster ; David Case ;
1 1
2
Jeffrey Peng ; University of Notre Dame, Notre Dame, IN; Center for Biophysics &
3
4
Computational Biology, Philadelphia, PA; Chevron Energy Tech. Co., Richmond, CA; Rutgers
University, Piscataway, NJ ........................................................................................................................... 33
TOB 11:10-11:35
Solution NMR Techniques for the Characterization of Chaperone–Substrate Complexes;
Sebastian Hiller; Björn M. Burmann; Morgane Callon; Biozentrum, Basel, Switzerland ............................... 33
TOB 11:35-12:00
Mapping Allosteric Networks through the Covariance and Projection Analyses of NMR
Chemical Shifts: Methods and Applications; Giuseppe Melacini; McMaster University,
Hamilton, Canada ......................................................................................................................................... 33
TOB 12:00-12:15
Probing the Mechanism of Fibril Formation in D76N β-2-Microglobulin with Ultra-Fast
1
1
1
Magic-Angle Spinning; Tanguy Le Marchand ; Loren Andreas ; Emeline Barbet-Massin ;
1
1
2
2
3
Michael Knight ; Hugh Dannatt ; Stefano Ricagno ; Martino Bolognesi ; Sofia Giorgetti ; Vittorio
4
5
1 1
Bellotti ; Lyndon Emsley ; Guido Pintacuda ; Institut des Sciences Analytiques, Lyon, France;
2
3
4
Dept of Biosciences, Milano, Italy; Dept of Molecular Medicine, Pavia, Italy; Univ College
5
London, London, UK; Ecole Polytechnique Federale de Lausanne, Lausanne, Switzerland (also
poster 478 on Mon/Tues) ............................................................................................................................. 33
TOB 12:15-12:30
19
F NMR Reveals Multiple Conformations at the Dimer Interface of the Non-Structural
1
1
Protein 1 Effector Domain from Influenza A Virus; James Aramini ; Keith Hamilton ; Li-Chung
1
1
2
2
3
1
Ma ; G.V.T. Swapna ; Paul Leonard ; John Ladbury ; Robert Krug ; Gaetano Montelione ;
1
2
CABM, Rutgers University, Piscataway, NJ; University of Texas MD Anderson Center,
3
Houston, TX; University of Texas, Austin, TX (also poster 479 on Mon/Tues)............................................ 33
10:45 –AM – 12:30 PM, TUESDAY MORNING
METABOLOMICS AND SMALL MOLECULES
Yulan Wang, presiding
Chapel
TOC 10:45-11:10
Making NMR the Method of Choice in Metabolomics; David Wishart; University of Alberta,
Edmonton, Canada ...................................................................................................................................... 34
TOC 11:10-11:35
Metabolomics and Drug Discovery; Robert Powers; Teklab Gebregiworgis; Steven Halouska;
Shulei Lei; Darrell Marshall; Emily Snell; Bradley Worley; Bo Zhang; University of NebraskaLincoln, Lincoln, NE...................................................................................................................................... 34
TOC 11:35-12:00
Defining Metabolomes: Roles of NMR and Challenges; Huiru Tang; Cas Key Lab Mr Biol
Syst, Wuhan Inst Phys Math, Wuhan ........................................................................................................... 34
TOC 12:00-12:15
Ultrafast Double-Quantum NMR Spectroscopy; Adrien Le Guennec ; Laetitia Rouger ; Boris
2
3
3
1
2
Gouilleux ; Ilya Kuprov ; Malcolm Levitt ; Stefano Caldarelli ; Patrick Giraudeau ; Jean-Nicolas
1 1
2
Dumez ; ICSN - CNRS, Gif-Sur-Yvette, France; Université de Nantes, Nantes Cedex 03, N/A;
3
Southampton University, Southampton, UK ................................................................................................ 34
TOC 12:15-12:30
HOBS: Broadband Homonuclear Decoupled Band-Selective NMR Experiments with Full
Sensitivity; Laura Castañar Acedo; Albert Vigili; Teodor Parella; Universitat Autónoma
Barcelona, Cerdanyola Del Vallés, Barcelona, Spain (also poster 480 on Mon/Tues) ................................. 34
1
2
12:30 – 2:00 PM
Lunch Break
2:00 – 3:45 PM, TUESDAY AFTERNOON
POSTER SESSION, Fireside Pavilion
Posters begin on page 47. Authors of even-number spaces (002, 004, 008, etc) present on Tuesday and Thursday.
“Take Me Home” Nibbles
Page 19
TUESDAY, CONTINUED
4:00 – 5:50 PM, TUESDAY AFTERNOON
NMR AND COMPUTATION IN STRUCTURE CALCULATION
Rafael Bruschweiler, presiding
Merrill Hall
TOD 4:00-4:25
Abstract Page
1, 2
Bayesian Inference for Biomolecular Structure Determination; Michael Habeck ;
1
2
University of Göttingen, Göttingen, Germany; Max Planck Institute for Biophysical Chemistry,
Göttingen, Germany ..................................................................................................................................... 35
TOD 4:25-4:50
Hybrid Approaches for Protein Structure Determination Combining Computational
Modeling with Sparse NMR Restraints; Gaetano Montelione; Rutgers University, Piscataway,
NJ ................................................................................................................................................................. 35
TOD 4:50-5:05
Developing Force Fields for the Accurate Simulation of both Ordered and Disordered
1
1
1
1, 2 1
Protein States; Paul Robustelli ; Stefano Piana ; Alexander Donchev ; David Shaw ; D.E.
2
Shaw Research, New York, NY; Columbia University, New York, NY ........................................................ 35
TOD 5:05-5:20
Advances in Modeling the Structures of Biomolecular Assemblies from NMR and Cryo-EM
1
5
4
6
Data; Nikolaos Sgourakis ; Jean-Philippe Demers ; Omry Morag ; Birgit Habenstein ; Antoine
3
3
3
4
3
2
Loquet ; Suresh Kumar Vasa ; Stefan Becker ; Amir Goldbourt ; Adam Lange ; David Baker ;
1
2
3
NIDDK, NIH, Bethesda, MD; University of Washington, Seattle, WA; Max Planck Institute,
4
5
Goettingen, Germany; Tel Aviv University, Tel Aviv, N/A; Max-Planck Institute BPC, Göttingen,
6
Germany; Institut de Biologie et Chimie des Proteines, Lyon, France ........................................................ 35
TOD 5:20-5:35
Probing the Structural and Dynamical Effects of the Charged Residues of the TZF Domain
of TIS11d; Brittany Morgan; Laura Deveau; Francesca Massi; University of Massachusetts,
Worcester, MA (also poster 481 on Mon/Tues) ............................................................................................ 35
TOD 5:35-5:50
A Statistical Torsion Angle Potential Improves the Quality of NMR-based RNA Structures;
Guillermo Bermejo; Marius Clore; Charles Schwieters; National Institutes of Health, Bethesda,
MD (also poster 482 on Mon/Tues) .............................................................................................................. 35
4:00 – 5:50 PM, TUESDAY AFTERNOON
NOVEL MRI APPLICATIONS
Adrian Carpenter, presiding
Chapel
TOE 4:00-4:25
Translational Imaging of Fat Metabolism; S. Sendhil Velan; Singapore Bioimaging
Consortium, Singapore, Singapore .............................................................................................................. 36
TOE 4:25-4:50
Metabolic and Molecular Imaging by Hyperpolarized Magnetic Resonance; Arnaud
Comment; Ecole Polytechnique Fédérale de Lausanne, Lausanne, Switzerland......................................... 36
TOE 4:50-5:05
High Resolution 3D Hyperpolarized C Imaging Techniques; Eugene Milshteyn ; Cornelius
1
2
1
1
1
1
von Morze ; Galen Reed ; Hong Shang ; Peter Shin ; Zihan Zhu ; John Kurhanewicz ; Robert
1
1 1
2
Bok ; Daniel Vigneron ; UCSF, San Francisco, California; Heartvista, Menlo Park, CA ............................ 36
TOE 5:05-5:20
Dynamic in vivo Free Radical Imaging with Overhauser-Enhanced MRI; Mathieu
1, 2
3
1, 2
1, 4
3, 5
Sarracanie ; Fanny Herisson ; Najat Salameh ; David Waddington ; Cenk Ayata ;
1, 5 1
Matthew Rosen ; MGH/A.A. Martinos Center for Biomedical Imaging, Charlestown, MA;
2
3
Department of Physics, Harvard University, Cambridge, MA; Neurovascular Research Lab,
4
5
MGH, Charlestown, MA; School of Physics, University of Sydney, Sydney, Australia; Harvard
Medical School, Boston, MA (also poster 481 on Mon/Tues) ....................................................................... 36
TOE 5:20-5:35
An Optimal Pulse for Fluid-Suppressed Sodium Knee MRI at 7 T; Jae-Seung Lee; Ding Xia;
Ravinder Regatte; Department of Radiology, New York University, New York, NY ..................................... 36
TOE 5:35-5:50
Group Sparse Reconstruction of Highly Undersampled Echo Planar Correlated
Spectroscopic Imaging Scan: Application to Human Calf; Neil Wilson; Brian Burns; Zohaib
Iqbal; M. Albert Thomas; UCLA, Los Angeles, CA (also poster 484 on Mon/Tues) ...................................... 36
13
1
7:00 PM, TUESDAY EVENING
PANEL DISCUSSION ON SUSTAINABILITY AND SERVICE NEEDS FOR THE NMR COMMUNITY
Chad Rienstra, presiding
Chapel
Page 20
WEDNESDAY, APRIL 22
8:30 – 10:15 AM, WEDNESDAY MORNING
ELECTRON MEETS NUCLEUS
Song-i Han, presiding
Merrill Hall
WOA 8:30-8:55
Abstract Page
Dynamic Nuclear Polarization with Endogenous Polarizing Agents; Björn Corzilius; Goethe
University, Frankfurt Am Main, Germany...................................................................................................... 37
WOA 8:55-9:20
Recent Insights in Overhauser DNP at 0.3 and 3 Tesla; Marina Bennati; MPI for Biophysical
Chemistry, Göttingen, Germany ................................................................................................................... 37
WOA 9:20-9:45
Dynamic Nuclear Polarization (DNP) with MAS for biomolecular Solid-State NMR; Kent
Thurber; Wai-Ming Yau; Robert Tycko; National Institutes of Health, Bethesda, MD ................................... 37
WOA 9:45-10:00
Local and Bulk 13C Hyperpolarization in NV-Centered Diamonds at Variable Fields and
1
1
2
Orientations; Gonzalo Agustin Alvarez ; Christian Oliver Bretschneider ; Ran Fischer ; Paz
2
3
4
5
2
1
London ; Hisao Kanda ; Shinobu Onoda ; Junichi Isoya ; David Gershoni ; Lucio Frydman ;
1
2
3
Weizmann Institute of Science, Rehovot, Israel; Technion, Haifa, Israel; National Institute for
4
5
Materials Science, Tsukuba, Japan; Japan Atomic Energy Agency, Takasaki, Japan; University
of Tsukuba, Tsukuba, Japan (also poster 470 on Wed/Thurs) ..................................................................... 37
WOA 10:00-10:15 Room-Temperature in situ Nuclear Spin Hyperpolarization from Optically-Pumped
1, 2
1, 2
Nitrogen Vacancy Centers in Diamond; Jonathan P King ; Keunhong Jeong ;
1, 2
1, 2
1
1, 2
1
Christophoros Vassiliou ; Chang Shin ; Ralph Page ; Claudia Avalos ; Haijing Wang ; Alex
1, 2 1
2
Pines ; Department of Chemistry, UC Berkeley, CA; Materials Sciences Division, LBNL,
Berkeley, CA (also poster 471 on Wed/Thurs) ............................................................................................. 37
10:15 – 10:45 AM
Break
Page 21
WEDNESDAY, CONTINUED
10:45 AM – 12:30 PM, WEDNESDAY MORNING
BIOLIQUIDS
Wolfgang Jahnke, presiding
Merrill Hall
Abstract Page
WOB 10:45-11:10 Kinetics Matter: Elucidation the Mechanism of Transcriptional Riboswitches by NMR;
Harald Schwalbe; Univ of Frankfurt, Frankfurt, Germany ............................................................................. 38
13
WOB 11:10-11:35 New Methods based on C Direct Detection to Study Intrinsically Disordered Proteins;
Isabella C. Felli; CERM University of Florence, Sesto Fiorentino (Florence), Italy ....................................... 38
1
1
WOB 11:35-12:00 Testing the Multidrug Transport Mechanism of EmrE; Emma Morrison ; Supratik Dutta ;
1
1
1
1, 2 1
Anne Robinson ; Greg Dekoster ; Chao Wu ; Katherine Wildman ; Washington University,
2
Saint Louis, MO; University of Wisconsin, Madison, WI .............................................................................. 38
WOB 12:00-12:15 Transient Complexes Observed by Paramagnetic Relaxation Enhancement between
Ntr
Enzyme 1 and NPr Prevent Crossover between Phosphorylation Pathways; Madeleine
1
2
3
4
1
Strickland ; Ann Marie Stanley ; Guangshun Wang ; Susan Buchanan ; Alan Peterkofsky ; Nico
1 1
2
3
Tjandra ; NHLBI, NIH, Bethesda, MD; NIGMS, NIH, Bethesda, MD; Nebraska Medical Center,
4
Omaha, NE; NIDDK, NIH, Bethesda, MD (also poster 472 on Wed/Thurs) ................................................ 38
WOB 12:15-12:30 NMR to Measure Molecular-Level Curvature of Membranes by Proteins and Lipids; Adrian
Draney; Sean Smrt; Justin Lorieau; University of Illinois, Chicago, IL (also poster 473 on
Wed/Thurs)................................................................................................................................................... 38
10:45 AM – 12:30 PM, WEDNESDAY MORNING
EXOTICA
Sophia Hayes, presiding
Chapel
WOC 10:45-11:10 Ultra-Precise NMR-Magnetometers for High Fields; Peter Bluemler; Anna Nikiel; Andreas
Maul; Sergei Karpuk; Ernst Wilhelm Otten; Werner Heil; Institute of Physics, Mainz, Germany .................. 38
WOC 11:10-11:35 What NMR Can Tell Us about Metal Organic Frameworks; Jeffrey Reimer; UC Berkeley,
Berkeley, CA ................................................................................................................................................ 39
WOC 11:35-12:00 Synchronous Hyperpolarization and NMR of Xe Gas; Thad Walker; Anna Korver; Daniel
Thrasher; Michael Bulatowicz; Univ. of Wisconsin-Madison, Madison, WI ................................................... 39
WOC 12:00-12:15 Phosphorus-31 MRI of Hard and Soft Solids using Quadratic Echo Line-Narrowing; Sean
Barrett; Yale University Physics Dept., New Haven, CT............................................................................... 39
1, 2
1
WOC 12:15-12:30 The Principle of Reciprocity in Conductors; Andrew Ilott ; Mohaddese Mohammadi ; Hee
2
3
3
1 1
Jung Chang ; Nicole M. Trease ; Clare P. Grey ; Alexej Jerschow ; New York University, New
2
3
York, NY; Stony Brook University, Stony Brook, NY; University of Cambridge, Cambridge, UK ............... 39
12:30 – 2:00 PM, Lunch Break
2:00 – 3:45 PM, WEDNESDAY AFTERNOON
POSTER SESSION, Fireside Pavillion
Posters begin on page 47. Authors of odd-number spaces (001, 003, 005, etc) present on Monday and Wednesday.
Castroville Nibbles
4:00 – 6:00 PM
TUTORIAL SESSION, WEDNESDAY AFTERNOON
Albert Thomas, presiding
Merrill Hall
WOD 4:00 – 4:40
Using Solution State NMR to Understand the Conformational Behavior of Intrinsically Disordered
Proteins; Martin Blackledge; IBS Grenoble
WOD 4:40 – 5:20
You Spin Me Right Round: Tensors and Rotations in NMR; Leonard Mueller; University of California,
Riverside
WOD 5:20 – 6:00
Insights into Ultra High-Field NMR Magnet Technology; Gerhard Roth; Bruker BioSpin GmbH
Page 22
THURSDAY, April 23
8:30 – 10:05 AM, THURSDAY MORNING
METHODS DEVELOPMENT IN MRI
Daniel Vigneron, presiding
Merrill Hall
ThOA 8:30-8:55
Frequency- and Gradient-Modulated MRI: Imaging with Extreme Field Inhomogeneity;
Michael Garwood; Albert Jang; Naoharu Kobayashi; Sung-Min Sohn; Thomas Vaughan;
University of Minnesota, Minneapolis, MN
Abstract Page
39
;
ThOA 8:55-9:20
New Directions for Brain MRI Hardware and Acquisition; Lawrence L. Wald MGH Martinos
Center, Charlestown, MA; Harvard-MIT Division of Health Sciences and Tech., Cambridge, MA
ThOA 9:20-9:35
A Robust Suite of Fast and Ultrafast Methods for In Vivo Spectroscopy Imaging of pre1
1, 2
1, 3
Targeted Metabolic Peaks; Amir Seginer ; Zhiyong Zhang ; Noam Shemesh ; Rita
1,
1 1
2
Schmidt ; Lucio Frydman ; Weizmann Institute, Rehovot, Israel; Xiamen University, Xiamen,
3
4
China; Champalimaud Centre for the Unknown, Lisbon, Portugal; Leiden University Medical
Center, Leiden, The Netherlands (also poster 474 on Wed/Thurs) .............................................................. 40
ThOA 9:35-9:50
Isolated Amide Proton CEST Contrast at 7 T Correlates with Contrast-Enhanced T1w1
1
1
images of Tumor Patients; Johannes Windschuh ; Steffen Goerke ; Jan-Eric Meissner ;
2
1
1 1
Alexander Radbruch ; Peter Bachert ; Moritz Zaiss ; German Cancer Research Center,
2
Heidelberg, Germany; University of Heidelberg Medical Center, Heidelberg, Germany (also
poster 475 on Wed/Thurs) ............................................................................................................................ 40
ThOA 9:50-10:05
Magnetic Resonance Imaging of Metabolically Labeled Glycans using Hyper-CEST Xenon
Biosensors in a Live-Cell Bioreactor; Christopher Witte; Honor Rose; Vera Martos Riaño;
Stefan Reinke; Stefan Klippel; Christian Hackenberger; Leif Schröder; Leibniz-Institut für
Molekulare Pharmakologie, Berlin, Germany (also poster 476 on Wed/Thurs) ............................................ 40
39
10:05 – 10:45 AM
Break
Page 23
THURSDAY, continued
10:15 AM – 12:35 PM, THURSDAY MORNING
DNP: METHODS AND APPLICATIONS
Melanie Rosay, presiding
Merrill Hall
Abstract Page
ThOB 10:45-11:10 Mechanistic Studies of Dynamic Nuclear Polarization; Joanna R. Long; University of Florida,
Gainesville, FL.............................................................................................................................................. 40
ThOB 11:10-11:35 Dissolution DNP: Hardware and Methodology; Fabian Jähnig; Marcin Krajewski; Michael
Batel; Sebastian Kozerke; Matthias Ernst; ETH Zurich, Zurich, Switzerland ................................................ 40
ThOB 11:35-11:50 Hybrid Polarizing Solids for Pure Hyperpolarized Liquids through Dissolution Dynamic
1
2
2
2
Nuclear Polarization; David Gajan ; Aurélien Bornet ; Basile Vuichoud ; Jonas Milani ; Roberto
3
4
4
4
5
Melzi ; Henri A. van Kalkerendd ; Laurent Veyre ; Chloé Thieuleux ; Matthew P. Conley ;
5
5
1
5
Wolfram R. Gruning ; Martin Schwarzwalder ; Anne Lesage ; Christophe Copéret ; Geoffrey
2, 6
2
2 1
2
Bodenhausen ; Lyndon Emsley ; Sami Jannin ; ENS Lyon, Villeurbanne, France; EPFL,
3
4
Lausanne, Switzerland; Bruker Italia S.r.l, Milano, Italy; Université de Lyon, Lyon, France;
5
6
ETHZ, Zurich, Switzerland; ENS, Paris, France (also poster 477 on Wed/Thurs) ..................................... 40
ThOB 11:50-12:05 Efficient Dynamic Nuclear Polarization at 800 MHz with Trityl-Nitroxide Biradicals;
Guinevere Mathies; MIT, Francis Bitter Magnet Laboratory, Cambridge, MA .............................................. 41
ThOB 12:05-12:20 Insights into DNP Mechanisms from Localized Biradicals in the Dilute Limit; Rivkah
Rogawski; Ivan Sergeyev; Yongjun Li; Virginia Cornish; Ann McDermott; Columbia University,
New York, NY (also poster 478 on Wed/Thurs)............................................................................................ 41
ThOB 12:20-12:35 -in situ Rapid Melt DNP and Supercritical Overhauser DNP, New Approaches towards
Inline 1H NMR Detection of Low Concentration Metabolites in microfluidic flow; Jan Van
Bentum; Manvendra Sharma; Gerrit Janssen; Jim Leggett; Michael Tayler; Bas van Meerten;
Arno Kentgens; IMM, Radboud University, Nijmegen, Netherlands (also poster 479 on
Wed/Thurs)................................................................................................................................................... 41
10:45 AM – 12:30 PM, THURSDAY MORNING
COMPUTATIONAL NMR: PREDICTING SPECTRA AND CHEMICAL SHIFTS
Rafael Bruschweiler, presiding
Chapel
ThOC 10:45-11:10 Estimating Chemical Shifts from Protein and Nucleic Acid Structures; David Case; Rutgers
University, Princeton, NJ .............................................................................................................................. 41
1, 2
ThOC 11:10-11:35 Numerical Simulations of Solid-State NMR Experiments; Zdeněk Tošner ; Niels Chr.
1
1 1
2
Nielsen ; Thomas Vosegaard ; Aarhus University, Aarhus, Denmark; Charles University,
Prague, Czech Republic ............................................................................................................................... 41
1
ThOC 11:35-12:00 SpinDrops: Visualizing the State and Dynamics of Coupled Spin Systems; Ariane Garon ;
1
1
2
1
1, 2 1
Robert Zeier ; David Leiner ; Niklas J Glaser ; Michael Tesch ; Steffen Glaser ; Technical
2
Univ. Munich, Garching, Germany; GlaserSystems, Garching, Germany ................................................... 41
ThOC 12:00-12:15 Monitoring the Refinement of Crystal Structures with Solid-State NMR Data – a Path to
Ultra-High Resolution Crystal Structures? Jim Harper; University of Central Florida, Orlando,
FL ................................................................................................................................................................. 42
1
ThOC 12:15-12:30 A Revised NNLS Approach to High-Resolution NMR Relaxometry; Robert J. Klingler ; Klaus
2 1
2
Woelk ; Argonne National Laboratory, Argonne, IL; Missouri S&T, Rolla, MO (also poster 480
on Wed/Thurs).............................................................................................................................................. 42
12:30 – 2:00 PM
Lunch Break
2:00 – 3:45 PM, THURSDAY AFTERNOON
POSTER SESSION, Fireside Pavilion
Posters begin on page 47. Authors of even number spaces (002, 004, 008, etc) present on Tuesday and Thursday.
Ice Cream Social
Page 24
THURSDAY, continued
4:00 – 6:00 PM, THURSDAY AFTERNOON
BIOSOLIDS II
Chad Rienstra, presiding
Merrill Hall
ThOD 4:00-4:25
Abstract Page
Advances in MAS Solid-State NMR using Deuterated Microcrystalline Protein Samples;
Bernd Reif; TU Munchen, Garching, Germany ............................................................................................. 42
ThOD 4:25-4:50
Delving into the Unknown: Understanding How the Molecular Structure of Tissues Drives
1
2
1
1
Cell Behaviour; Melinda Duer ; Wing Ying Chow ; Rakesh Rajan ; Veronica Wong ; David G
1
1
1
1
1
1
Reid ; Dominique Bihan ; Richard Farndale ; Chris Forman ; David Wales ; Roger Brooks ;
1
2
University of Cambridge, Cambridge, N/A; Leibniz Institute for Molecular Pharmacology, Berlin,
Germany....................................................................................................................................................... 42
ThOD 4:50-5:15
Perspectives for Proton-Detected Solid-State NMR; Sheng Qi Xiang; Suresh Kumar Vasa;
Petra Rovó; Karin Giller; Stefan Becker; Rasmus J. Linser; Max Planck Institute for Biophysical
Chemistry, Göttingen, Germany ................................................................................................................... 42
ThOD 5:15-5:30
Line-Broadening in Low Temperature Solid-State NMR Spectra of Fibrils; Thomas Bauer ;
1
1
1
1
1
Claudio Dotta ; Livia Balacescu ; Julia Gath ; Andreas Hunkeler ; Matthias Ernst ; Anja
2
1 1
2
Böckmann ; Beat Meier ; ETH Zurich, Zurich, Switzerland; IBCP-CNRS, Lyon, France (also
poster 481 on Wed/Thurs) ............................................................................................................................ 43
ThOD 5:30-5:45
Catalytic Roles of βLys87 in Tryptophan Synthase: N Solid State NMR Studies; Bethany
G. Caulkins; Chen Yang; Michael F. Dunn; Leonard J. Mueller; University of California Riverside,
Riverside, CA (also poster 482 on Wed/Thurs) ............................................................................................ 43
ThOD 5:45-6:00
Reclaiming Resolution in DNP-SSNMR: Assignments and Distances from Higher1
2
3
4
Dimensional Experiments; Ivan Sergeyev ; Boris Itin ; Rivkah Rogawski ; Guohua Lv ; David
4
3 1
Eliezer ; Ann Mcdermott ; Columbia University / New York Structural Biology, New York, New
2
3
York; New York Structural Biology Center, New York, NY; Columbia University, New York, New
4
York; Weill Cornell Medical College, New York, NY (also poster 483 on Wed/Thurs)................................. 43
1
15
4:00 – 6:00 PM, THURSDAY AFTERNOON
INSTRUMENTATION
Jeff Reimer. presiding
Chapel
ThOE 4:00-4:25
Using Magnetic Coupling in High Resolution NMR Circuits; Toby Zens; Paul Bowyer; James
Finnigan; Brian Marsden; Victor Lim; Bob Taber; Agilent Technologies, Santa Clara, CA ........................... 43
ThOE 4:25-4:50
Probing the Influence of Nuclear Spins on the Magneto-Optoelectronic Properties of piConjugated Polymers; Christoph Boehme; University of Utah, Salt Lake City, UT .................................... 43
ThOE 4:50-5:15
Closed-Cycle Helium-Cooling MAS NMR Probe System for Dynamic Nuclear Polarization
1
2
2
3
at 16.4 T; Yoh Matsuki ; Toshitaka Idehara ; Yoshinori Tatematsu ; Jagadishwar Sirigiri ; Shinji
4
1 1
2
Nakamura ; Toshimichi Fujiwara ; Osaka University, Suita, Japan; University of Fukui, Fukui,
3
4
JP; Bridge12 Technologies Inc., Framingham, MA; JEOL Resonance Inc., Akishima, JP ........................ 44
ThOE 5:15-5:30
Pre-clinical Magic Angle Field Spinning MRI magnet for localized NMR spectroscopy;
Javier Alonso Valdesueiro; Cedric Hugon; Anne Soleilhavoup; Angelo Guiga; Guy Aubert;
Dimitrios Sakellariou; CEA Saclay, Gif-Sur-Yvette, France .......................................................................... 44
ThOE 5:30-5:45
1.02 GHz LTS/HTS NMR: I. Development to Overcome the Limitation of Magnetic Field
1
2
2
2
1
Strength; Masato Takahashi ; G. Nishijima ; S. Matsumoto ; K. Hashi ; S. Iguchi ; Y.
1
1
3
3
4
4
4
Yanagisawa ; H. Maeda ; T. Miki ; K. Saito ; R. Tanaka ; T. Nemoto ; T. Miyamoto ; H.
4
2
2
2
2 1
2
Suematsu ; T. Noguchi ; S. Ohki ; A. Goto ; T. Shimizu ; RIKEN CLST, Yokohama, Japan; Natl
3
4
Inst for Materials Science, Tsukuba, Japan; Kobe Steel Ltd., Kobe, Japan; JEOL Resonance
Inc., Akishima, Japan (also poster 484 on Wed/Thurs) ................................................................................ 44
ThOE 5:45-6:00
First NMR Results from an H/X/Y/e- CryoMAS-DNP Probe Compatible with Closed-loop
1
1
1
1
Spinning at 30 K; John Staab ; JB Spitzmesser ; Daniel Arcos ; George Entzminger ; Judy
1
1
1
1
1
2
Doty ; Vince Cothran ; Marc Bremmer ; Glenn Doty ; David McCree ; Hiroto Suematsu ; Laura
1
1
1 1
2
Holte ; Paul Ellis ; F. David Doty ; Doty Scientific, Inc., Columbia, SC; JEOL Resonance Inc.,
Tokyo, Japan ................................................................................................................................................ 44
Page 25
THURSDAY EVENING
6:30 – 8:00 PM
Conference Dinner, ticket required
8:00 – 9:00 PM, THURSDAY EVENING
After Dinner Program, Teresa Carlomagno, presiding
All are welcome. No ticket is needed.
Merrill Hall
Gerhard Wagner; Harvard University Medical School
Winning the Lottery . . .
or
Where the Cool Things Are
AWARD PRESENTATIONS
Ritchey Travel Award: Laura Castañar Acedo, Universitat Autonòma de Barcelona
JMR Awards presented by Lucio Frydman, Editor in Chief
sponsored by Elsevier Science
•
Andrew Ilott, New York University
•
Guilliame Mas, Structural Biology Institute
•
Guinevere (Jennifer) Mathies, MIT
ENC Executive Committee Election Results
Return to our roots: Pittsburgh 2016
th
Chad Rienstra, Chair 57 ENC
Raffle of valuable prizes from the cards returned with all vendor stickers. You must be present to win.
Page 26
FRIDAY, APRIL 24
8:30 – 10:15 AM, FRIDAY MORNING
DYNAMICS: METHODS AND APPLICATIONS
Teresa Carlomagno, presiding
Merrill Hall
Abstract Page
FOA 8:30-8:55
Binding Pathways of Transient Protein Complexes Studied by NMR Relaxation Dispersion
Experiments; Anthony K Mittermaier; Mcgill University, Montreal, Canada ................................................ 44
FOA 8:55-9:20
Dynamic Signatures of Active and Inhibited Protein Kinase A using NMR Spectroscopy;
Gianluigi Veglia; University of Minnesota, Minneapolis, MN ......................................................................... 44
FOA 9:20-9:45
Observing Short-Lived States in Proteins by Solid-State NMR: New Methods Provide
Insight into Functional Dynamics of a Half-Megadalton Enzymatic Complex; Paul Schanda;
Institut de Biologie Structurale, Grenoble, France ........................................................................................ 45
FOA 9:45-10:00
Characterizing Potassium Binding-Sites in Proteins by 15NH4+ NMR Spectroscopy;
Nicolas Werbeck; D. Flemming Hansen; ISMB, Univ. College London, London, United Kingdom ............... 45
FOA 10:00-10:15
Simultaneous Characterization of Spin Dynamics at Both Fast (ps-ns) and Slow (μs-ms)
Time Scales using Adiabatic Spin-lock Experiments; Fa-An Chao; R. Andrew Byrd; National
Cancer Institute, Frederick, MD .................................................................................................................... 45
10:15 – 10:45 AM, Break
10:45 AM – 12:30 PM, FRIDAY MORNING
THE QUEST FOR A BETTER SIGNAL: IMPROVING SENSITIVITY AND RESOLUTION
Jeffrey Hoch, presiding
Merrill Hall
FOB 10:45-11:10
Enhancing the Resolution of Proton-detected NMR Spectra by Spatially-selective
Excitation; Klaus Zangger; N.Helge Meyer; Simon Glanzer; Nina Gubensäk; Johannes Mauhart;
University of Graz, Graz, Austria .................................................................................................................. 45
FOB 11:10-11:35
Parahydrogen Induced Polarization by Pairwise Replacement Catalysis; Clifford R. Bowers ;
1, 2
1
3
3, 4
3
Ronghui Zhou ; Evan Zhao ; Wei Cheng ; Luke Neal ; Haibin Zheng ; Helena Hagelin3 1
2
Weaver ; Chemistry, University of Florida, Gainesville, Florida; Colgate-Palmolive Technology
3
Center, Piscataway, New Jersey; Chemical Engineering, University of Florida, Gainesville, FL;
4
NC State University, Raleigh, NC................................................................................................................ 45
FOB 11:35-12:00
Theorems for the Sensitivity Advantages of Nonuniform Sampling; David Rovnyak ; Melissa
1
3
5
4
2
Palmer ; Christopher Suiter ; Geneive E. Henry ; James Rovnyak ; Jeffrey C. Hoch ; Tatyana
3 1
2
Polenova ; Bucknell University, Lewisburg, PA; Univ of Connecticut Health Ctr, Farmington;
3
4
5
University of Delaware, Newark, NJ; University of Virginia, Charlottesville, VA; Susquehanna
University, Selinsgrove, PA .......................................................................................................................... 46
FOB 12:00-12:15
Slice-Selective NMR : Toward Fully Resolved Correlation Spectroscopy; Nicolas Giraud;
Universite Paris-Sud, Orsay, France ............................................................................................................ 46
FOB 12:15-12:30
Quantitative Trace Analysis of Complex Mixtures Using SABRE Hyperpolarization; Nan
Eshuis; Bram J. A. van Weerdenburg; Martin C. Feiters; Floris P.J.T. Rutjes; Sybren S.
Wijmenga; Marco Tessari; Radboud University, Nijmegen, Netherlands ..................................................... 46
1
1
Adjourn
Page 27
Page 28
ABSTRACTS OF TALKS
10:45 AM – 12:30 PM, MONDAY MORNING
Bioliquids: Challanging Systems
Tatyana Polenova, presiding
Merrill Hall
MOB 10:45-11:10
Molecular Chaperones in Action
Charalampos Babis Kalodimos
Rutgers University, Piscataway, NJ
Molecular chaperones are necessary for maintaining a
functional proteome in the cell by preventing the aggregation
of unfolded proteins and/or assisting with their folding. Despite
the central importance of the binding of chaperones to
unfolded substrates, the structural basis of their interaction
remains poorly understood. The scarcity of structural data on
complexes between chaperones and unfolded client proteins
is primarily due to technical challenges originating in the
dynamic nature of these complexes.
I will discuss how NMR spectroscopy can be used as an
extremely powerful tool to determine the structural and
dynamic basis for the recognition and interaction of unfolded
proteins by molecular chaperones.
MOB 11:10-11:35
NMR and EPR as a Tool to Study the Assembly and
Structure of a Large Multicomponent
Protein-RNA Complex
1, 2
1
1
Olivier Duss ; Maxim Yulikov ; Erich Michel ; Gunnar
1
1
Jeschke ; Frederic H.-T. Allain
1
2
ETH Zurich, Zurich, Switzerland; The Scripps Research
Institute, La Jolla, CA
High-resolution structural information on RNA and its
functionally important complexes with proteins is dramatically
underrepresented compared with proteins but is urgently
needed for understanding cellular processes at the molecular
and atomic level. Here we present a combined NMR/ EPRbased protocol to help solving large RNA and protein–RNA
complex structures in solution and to study their
macromolecular assembly.
We used this approach to study the cooperative assembly
and determine the solution structure of the 70 kDa complex
consisting of the 72 nucleotides non-coding RNA RsmZ and
three homo-dimeric RsmE proteins, a complex which is
present in two conformations in solution and is important for
fine-tuning bacterial virulence.
MOB 11:35-12:00
Rapid and Accurate Assignment of Larger Protein
Resonances with Time-Shared Acquisition, Non-uniform
Sampling, and Covariance NMR.
Dominique Frueh; Subrata Mishra; Bradley Harden; Scott
Nichols; Andrew Goodrich
Johns Hopkins School of Medicine, Baltimore, MD
NMR spectra of large monomeric proteins suffer from
sensitivity losses, spectral crowding, and frequency
degeneracies, which impede assignment of NMR resonances.
Here, we present various strategies to overcome these
obstacles. Covariance NMR is used to combine the
information of multiple conventional 3D spectra into a single
4D array. Thus, a 4D-HsNsHN permits assignment of
sequential amide resonances by simple visualization of H/Ncorrelation planes. Likewise, residue-specific 4D-HmCmHN
maps directly pair methyl resonances with assigned amide
signals. Finally, NOESY resonances are assigned with a time-
shared experiment designed for optimal non-uniform sampling
15
13
N and
C
acquisition, which simultaneously provides
dispersed NOESY spectra with ultra-high resolution in all
dimensions. Methods are demonstrated on 37 kDa and 52
kDa nonribosomal peptide synthetase domains.
MOB 12:00-12:15
Studies of a 1 MDa Chaperonin in Action by Combined
NMR and EM Approaches
Guillaume Mas; Pavel Macek; Elodie Crublet; Christine
Moriscot; Schanda Paul; Schoehn Guy; Boisbouvier Jerome
Structural Biology Institute, Grenoble, France
The study of the assembling, structural and functional
properties of biomolecular nanomachines remains a
considerable practical challenge. NMR spectroscopy offers an
unique ability to monitor structural and dynamic changes in
real-time and at atomic resolution. However, the NMR studies
of large proteins and complexes has been a real challenge for
a long time. In this communication, I will present that a
combination of methyl specific labeling, optimized NMR
spectroscopy integrated with EM can be used to probe
different functional states and refolding cycle of a 1 MDa
active chaperonin. NMR allowed us to investigate in an
atomicand
time-resolved
manner
the
structural
rearrangement corresponding to the different states during the
functional cycle of a large biological machinery processing its
substrate.
MOB 12:15-12:30
Solution Structure of the 108 nt J-K Region from the
Encephalomyocarditis Virus IRES RNA
1
2
3
Shunsuke Imai ; Michael Durney ; Xiaobing Zuo ; Tatyana
4
4
2
Pestova ; Christopher Hellen ; Victoria D'Souza ;
1
Gerhard Wagner
1
2
Havard Medical School, Boston, MA; Harvard University,
3
Cambridge, MA; Argonne National Laboratory, Chicago, IL;
4
SUNY Downstate Medical Center, Brooklyn, NY
The structure of the 108-nucleotide J-K RNA region from the
internal ribosome entry site (IRES) of Encephalomyocarditis
virus (EMCV) was solved by solution NMR combined with
small angle X-ray scattering (SAXS). First, structures of three
domains isolated from J-K were determined. Second, the
structure of the A-bulge, which is not included in any of the
three domains, was characterized by adenosine specific
isotopically labeled J-K. Finally, the structure of full-length J-K
was solved by combining the fragment structures to satisfy
SAXS data as global restraint. The structure has a novel fold
that provides a basis for understanding how this region
interacts with the eukaryotic translation initiation factor eIF4G
and initiates translation of proteins needed for viral replication.
4:00 – 6:00 PM, MONDAY AFTERNOON
NMR in Chemical Biology and Drug Design
Ichio Shimada, presiding
Merrill Hall
MOD 4:00-4:25
NMR-aided Discovery of an Allosteric Bcr-Abl Inhibitor in
Clinical Trials for the Treatment of CML
Wolfgang Jahnke
Novartis Institutes for Biomedical Research, Basel,
Switzerland
The early lead finding stages in the discovery of a clinical
candidate for the treatment of chronic myelogenous leukemia
(CML) will be described. NMR spectroscopy played a critical
Page 29
ABSTRACTS OF TALKS
role in this process of fragment-based discovery, not only for
the screening of fragment libraries and the quantitative
assessment of structure-activity relationships (SAR), but also
for the characterization of evolved fragments by an NMRbased conformational assay. We will give a short tour through
the discovery process, highlighting the principles employed in
fragment-based drug discovery and medicinal chemistry
aimed at obtaining a clinical candidate with high potency and
selectivity, in order to provide a safe and efficacious treatment
for CML.
MOD 4:25-4:50
eNOE for Protein and Protein-Ligand Complex Studies
Roland Riek; Beat Voegeli; Julien Orts; Celestine Chi;
Dean Strotz; Marielle Wälti
ETH Zurich, Zurich, Switzerland
Proteins and protein-ligand complexes are inherently dynamic
systems interchanging between various substates. For a
detailed understanding of a protein’s function or the proteinligand interaction, the structural landscape at atomic
resolution is therefore required. Towards this goal we
introduced an ensemble-based structure determination
protocol that relies on the use of exact NOE (eNOE). The
applications to several protein and protein-ligand complexes
indicate the presence of correlated structural patterns.
In addition, inter-molecular eNOEs can be used for the fast
structural identification of the ligand-protein binding pocket
without any sequential assignment of the protein, but with the
request of having a homologues structure available. This
method is called NMR2 for NMR molecular replacement
reminiscent to the molecular replacement method in x-ray
crystallography.
MOD 4:50-5:15
Membrane Interaction and Conformational Equilibrium of
Nanodisc-tethered KRAS and its Oncogenic Mutants
1
2
1
Mitsu Ikura ; Mohammad Mazhab-Jafari ; Zhenhao Feng ;
1
1
Matthew J Smith ; Christopher B Marshall
1
2
Princess Margaret Cancer Centre, Toronto, CA; Hospital for
Sick Children, Toronto, CA
We use solution NMR spectroscopy to dissect the structure
and function of the oncogene product RAS protein, with
specific emphasis on understanding how oncogenic mutations
alter the RAS function. Our parallel and quantitative NMR
assays of RAS-effector interactions demonstrated that mutant
RAS G12V markedly influences properties of the RAS-effector
interaction network. As RAS is prenylated and functions on
the plasma membrane, we are particularly interested in
elucidating the behavior of RAS on membranes. We
employed the nanodisc technology to study the conformation
and dynamics of membrane-tethered KRAS. These NMRbased structural and functional studies of RAS provide novel
and unprecedented information on the RAS biology and help
develop new therapeutic strategies for human cancer.
MOD 5:15-5:30
Structural and Dynamic Features of F-recruitment Site
Driven Substrate Phosphorylation by ERK2
1
1
1
Andrea Piserchio ; Venkatesh Ramakrishnan ; Hsin Wang ;
2
3
4
2
Tamer Kaoud ; Boris Arshava ; Kaushik Dutta ; Kevin Dalby ;
1
Ranajeet Ghose
1
2
The City College of New York, New York, NY; University of
3
Texas, Austin, Austin, TX; The College of Staten Island,
4
Staten Island, NY; The New York Structural Biology Center,
New York, NY
Page 30
The F-recruitment site (FRS) of active ERK2 binds F-site
(Phe-x-Phe-Pro) sequences found downstream of the Ser/Thr
phospho-acceptor on substrates. We have used NMR
methods to analyze the interaction between active ERK2
(ppERK2), and an F-site-bearing substrate derived from the
transcription factor Elk-1. Engagement of the ppERK2 FRS by
the F-site sequence quenches slow dynamics involving the
ppERK2 activation-loop and the FRS. The F-site
phenylalanines are found to make critical contacts with
ppERK2 FRS, in contrast to the proline that has no significant
role. In addition, our results support a mechanism where
phosphorylation of the disordered N-terminal phosphoacceptor is facilitated by its increased productive encounters
with the ppERK2 active site due to docking of the proximal Fsite at the kinase FRS.
MOD 5:30-5:45
Ligand-Protein Screening by Long-Lived States of
Fluorine-19 Nuclei
1
1
1
Roberto Buratto ; Daniele Mammoli ; Aurélien Bornet ; Estel
1, 2
1
1
1
Canet ; Basile Vuichoud ; Jonas Milani ; Sami Jannin ;
1, 2
Geoffrey Bodenhausen
1
2
EPFL, Lausanne, Switzerland; ENS, Paris, France
The use of LLS for fragment screening allows one to
characterize binding of fragments with very weak affinities. By
exploiting the LLS behavior of a spy molecule, we have
demonstrated that it is possible to measure dissociation
constants as large as 12 mM.
We have also explored the combination of LLS screening with
dissolution-DNP. We performed DNP-enhanced screening by
measuring the LLS signal of a weak ligand using very low
concentrations of ligand and trypsin.
We are currently exploring LLS involving pairs of 19F nuclei.
We have observed a promising ratio TLLS/T1 = 4 and
measured a dramatic effect on the LLS lifetime due to the
presence of trypsin. Experiments aimed at quantifying
dissociation constants are in progress.
MOD 5:45-6:00
Real-Time Monitoring of Enzymatic Reactions in Living
Cells by NMR and Its Applications in Drug Discovery
Jun Hu
AstraZeneca, Waltham, MA
Understanding how protein function in the complex cellular
environment is a key challenge of modern biology. Here, we
report an NMR method that affords the ability to monitor the
meropenem hydrolysis by NDM-1 Escherichia coli cells. Our
cell-based NMR studies determine the IC50 of L-captopril and
EDTA inhibition in cells. We believe this new approach can
have generic utility for monitoring reactions involving diffusible
metabolites in other complex biological matrices and cellular
settings. Building on this study, we designed a cell-based
NMR screening platform. A potent NDM-1 inhibitor was
identified. This new screening approach has great potential to
be applied to targets in other cell types and challenging
targets in the cellular environment.
ABSTRACTS OF TALKS
4:00 – 6:00 PM, MONDAY AFTERNOON
Materials
Brad Chmelka, presiding
Chapel
MOE 4:00-4:25
35
Screening of Active Pharmaceutical Ingredients via Cl,
14
15
N and N Solid-State NMR
1
1
Robert W. Schurko ; Michael Jaroszewicz ; Andrew
1
1
1
Namespetra ; Anthony Sandre ; Marcel Hildebrand ; Hiyam
1
1
1
Hamaed ; Stanislav Veinberg ; Karen Johnston ; Lucio
2
3
4
5
Frydman ; Marek Pruski ; Takeshi Kobayashi ; Ivan Hung ;
5
Zhehong Gan
1
2
University of Windsor, Windsor, Canada; Weizmann
3
Institute, Rehovot, Israel; Ames Laboratory, Iowa State
4
University, Ames, IA; Iowa State University, Ames, IA;
5
NHMFL, Tallahassee, FL
The screening of solid phases of active pharmaceutical
ingredients (APIs) is of great importance to the
13
1
pharmaceutical industry. Conventional C and H NMR
experiments are typically applied for such systems, but have
limitations for the detection of impurities and study of dosage
35
forms. However, there are several nuclides, including Cl,
14
15
N and N, which are useful in NMR experiments for
identifying, differentiating and discovering solid APIs. In this
lecture, I will discuss developments and applications of (a)
35
Cl SSNMR for the characterization of HCl salts of APIs
(which constitute ca. 50% of all known APIs) and (b) a tandem
14
15
N/ N SSNMR approach for the study of nitrogen-containing
APIs (no isotopic enrichment required).
MOE 4:25-4:50
Applications in the Study of Technological and
Cultural Materials
1
1
1
1
Cecil Dybowski ; Jaclyn Catalano ; Anna Murphy ; Yao Yao ;
1
1
1
Sean Holmes ; Fahri Alkan ; Shelby Chan ; Nicholas
3
2
Zumbulyadis ; Silvia Centeno
1
2
University of Delaware, Newark, DE; The Metropolitan
3
Museum of Art, New York, NY; Independent Researcher,
Rochester, NY
We discuss the application of NMR to several solid-state
problems.
Prediction of chemical shielding tensors is
fundamental to inferring structure, and we discuss efforts to
use a cluster method to evaluate the structure/property
relationship for several different nuclei. We apply NMR
spectroscopy, along with other analytical techniques, to study
of a process that affects many paintings from the 15th through
the 20th century, the formation of lead soaps. We apply the
same NMR techniques to the study of polymorphic structure
of an active pharmaceutical ingredient in a medication. The
work has been supported by the U. S. National Science
Foundation under grants CHE-0956006, CHE-1139180, and
CHE-1139192.
MOE 4:50-5:15
DNP Enhanced Solid-State NMR Spectroscopy of
Materials
1, 2
Lyndon Emsley
1
ENS Lyon, Villeurbanne, France;
2
EPFL, Lausanne, Switzerland
We show how enhanced NMR spectroscopy can be achieved
by using DNP for surfaces and for bulk solids. We obtain over
a hundred-fold signal enhancement in systems from
mesoporous silicas to metal organic frameworks to
nanoparticles and cements, microparticulate solids or intact
pharmaceutical formulations.
In particular we will discuss results from high field (18.8 T)
MAS DNP and from fast MAS, and we will show how the
enhanced sensitivity provided by DNP enables the
determination of full three dimensional structures of
functionalism surfaces.
MOE 5:15-5:30
High Resolution Solid-State NMR of Highly Radioactive
Materials: A New Insight into the 5f-Chemistry of
Paramagnetic Compounds
Laura Martel; Chris Selfslag; Joseph Somers
JRC-ITU, Eggenstein Leopoldshafen, Germany
A massive interest has been lately devoted by the
improvement of solid-state magic-angle spinning (MAS) NMR
methods for the study of a broad range of paramagnetic
organic and inorganic materials. However, the analysis of
actinide-bearing compounds and their 5f-unpaired electrons
remained for a long time elusive mainly because of their wellknown high radiotoxicity. As materials, the interest in actinide
dioxides and mixed oxides is indisputable due to their use or
consideration as fuels and/or targets for the transmutation of
minor actinides in fast neutron reactors. They have thus been
the perfect targets for landing into this new area of
paramagnetic solid-state NMR.
Thanks to a dedicated effort enabling the handling of these
highly radioactive materials, their analysis using highresolution MAS NMR (>55 kHz) is now possible on a routine
basis (Figure 1). Here, we will present the atomic scale study
of a series of actinide dioxides, namely, ThO2, UO2, NpO2,
PuO2, and AmO2, using 17O NMR. The paramagnetic shifts
will be interpreted using an empirical approach and single-ion
model calculations. As an opening to this study, the recent
results obtained on uranium−neptunium
and uranium
plutonium mixed dioxides will be presented (Figure 2).
MOE 5:30-5:45
Dynamic Nuclear Polarization enhanced Solid State NMR
of Insensitive Nuclei: Oxygen-17 at Natural Abundance
and Low-gamma Yttrium-89
Frédéric Blanc
University of Liverpool, Liverpool, United Kingdom
Natural abundance 17O NMR of hydroxides and oxides could
be obtained in minutes only at 9.4 T by using indirect or direct
DNP, respectively at low temperature under static and MAS
conditions. The results open up a powerful method for rapidly
acquiring high signal-to-noise ratio solid-state NMR spectra of
17O and to probe sites on or near the surface, without the
need for isotope labeling. Solid-state NMR spectra of low
gamma nuclei such as 89Y can be acquired fairly quickly with
indirect DNP at 9.4 T. The detection of the 89Y NMR signals
from hydrated BaZr0.8Y0.2O2.9 allows the local yttrium (and
proton) environments present in these important protonic
conductors to be detected.
MOE 5:45-6:30
Mg NMR Studies of Mg-ion Battery Materials
1
1
3
Hao Wang ; Danielle Proffit ; Cheon Jung Kim ; Premkumar
1
2
2
3
Senguttuvan ; Victor Duffort ; Linda Nazar ; Jordi Cabana ;
1
1
1
Anthony Burrell ; John Vaughey ; Baris Key
1
2
Argonne National Laboratory, Lemont, IL; University of
Waterloo, Waterloo, Canada;
3
University of Illinois at Chicago, Chicago, IL
25
Page 31
ABSTRACTS OF TALKS
Multivalent-ion chemistries such as Mg-ion are emerging as
alternative battery systems to Li-ion. Current Mg-ion
chemistries are limited to relatively low voltages and relatively
low reversible specific capacities (1-2). Recent research on
potential high voltage Mg-ion cathode materials have
highlighted the need to understand structure activity
relationships and intercalation (3). Solid state NMR is a
powerful tool to investigate local structure and
insertion/intercalation phenomena, particularly for batteries as
6
7
shown for Li-ion chemistries with Li and Li NMR (4, 5). In
25
this work, despite the challenges of Mg NMR, our recent
efforts to characterize Mg environments in cathode materials
such as MgMn2O4 spinels, MgV2O5. The results will
summarize the effectiveness of the method in distinguishing
side reactions or undesirable conversion reactions.
MAS probe for NHMFL Series-Connected hybrid.
8:30 – 10:15 AM, TUESDAY MORNING
Biosolids I
Anne Lasage, presiding
Marrill Hall
TOA 8:30-8:55
Structure and Dynamics of HIV-1 Protein
Assemblies by MAS NMR
1, 2
1
1
Tatyana Polenova ; Manman Lu ; Christopher Suiter ;
1
1
1
Huilan Zhang ; Guangjin Hou ; Mingzhang Wang ; Rupal
1
1
1
3
Gupta ; Caitlin Quinn ; Xingyu Lu ; Jinwoo Ahn ; In-Ja
3
2, 4
Byeon ; Angela Gronenborn
1
2
University of Delaware, Newark, DE; Pittsburgh Center for
3
HIV Protein Interactions, Pittsburgh, PA; University of
4
Pittsburgh School of Medicine, Pittsburgh, PA; University of
Pittsburgh, Pittsburgh, PA
Formation of infectious HIV-1 virions occurs through the
maturation process, i.e., sequential proteolytic cleavage of
Gag polyprotein precursor into its constituent domains,
leading to the formation of conical capsid core that encloses
the viral RNA genome and complementary proteins. I will
present recent methodological developments that enable
atomic-resolution characterization of structure and dynamics
of HIV-1 protein assemblies comprised of Gag and its
cleavage products, by MAS NMR and hybrid methods. I will
discuss the role of conformational dynamics in HIV-1 CA
protein and Gag maturation intermediates in the assembly of
the capsid, viral maturation, and interactions with host cell
factors.
I will demonstrate the potential of emerging
methodologies, including fast-MAS and DNP, for resolution
and sensitivity enhancements in HIV-1 assemblies.
TOA 8:55-9:20
Structural studies of Y145Stop Prion Protein Amyloids
1
1
1
1
Theint Theint ; Philippe S. Nadaud ; Darryl Aucoin ; Zhe Qi ;
2
2
Krystyna Surewicz ; Witold K. Surewicz ;
1
Christopher P. Jaroniec
1
2
The Ohio State University, Columbus, OH; Case Western
Reserve University, Cleveland, OH
The results of our recent studies aimed at providing the
structural basis of strains and seeding specificities of
mammalian Y145Stop prion protein (PrP23-144) amyloids will
be presented. We find that mutations of specific amino acid
residues in the human protein alter the amyloid core
conformation to resemble that of either the mouse or hamster
amyloid, and that these mutations appear to be responsible
for the onset of amyloid polymorphism. We also present a
Page 32
preliminary structural model for human PrP23–144 amyloid
which provides initial insights into these observations.
TOA 9:20-9:45
MAS NMR Studies of Biomaterial Interfaces between
Bone-like Apatite and Its Regulatory
Proteins and Peptides
1
1
1
Gil Goobes ; Irina Matlahov ; Taly Iline-Vul ; Alex
1
2
1
Kulpanovich ; Elizabeth M. Y. Lee ; Yasmin Geiger ; Merav
1
1
2
Nadav-Tsubery ; Keren Keinan-Adamsky ; Jeffrey Gray
1
2
Bar Ilan University, Ramat Gan, ISRAEL; Johns Hopkins
University, Baltimore, MD
Osteocalcin (OC) and osteonectin (ON) are proteins
implicated with different roles during bone formation. OC is
essential for bone structure and ON is interfacing mineral and
bone cells signaling mineralization. The proteins were coprecipitated with hydroxyapatite and their effect on mineral
growth was analyzed via MAS NMR with XRD, TGA, ICP,
BET and TEM. The surface and bulk of growing
hydroxyapatite crystals, their structure and morphology and
the interface with the polypeptides are probed using
1
31
31
polarization build-up in 2D H- P HETCOR, P SEDRA and
13
31
C- P REDOR measurements showing differences imposed
by OC and by ON. The residues involved in interaction with
the mineral surface are inferred from experiments
complemented by models of interfaces between the mineral
crystal faces and biomolecules.
TOA 9:45-10:00
Structure of an RNA by Solid-State NMR
1
1
2
Alexander Marchanka ; Bernd Simon ; Gerhard Althoff ;
1
Teresa Carlomagno
1
2
EMBL, Heidelberg, Germany; Bruker BioSpin,
Rheinstetten, Germany
Nucleic acids and ribonucleoprotein (RNP) complexes play a
regulatory and functional role in cellular processes; as for
proteins, the elucidation of their activity mechanisms requires
knowledge of their structure. RNAs and RNPs are difficult to
crystallize, probably due to the conformational plasticity of the
RNA, while the use of solution-state NMR is limited by the
molecular weight. Solid-state NMR (ssNMR) is an attractive
alternative for the study of large biomolecular systems. Here
we report the first structure of an RNA determined solely by
ssNMR data, together with the methods developed for it. Our
strategy uses easy-to-produce nucleotide-type selectively
labeled RNAs and sensitive magnetization transfer schemes.
We expect this method to have a considerable impact in
structural biology of RNA.
TOA 10:00-10:15
The Capsid Model of Intact M13 Bacteriophage from MAS
NMR and Rosetta Modeling: A Quadrupled Hydrophobic
Viral Packing Epitope
1
2
1
Omry Morag ; Nikolaos Sgourakis ; Gili Abramov ; David
3
1
Baker ; Amir Goldbourt
1
2
Tel Aviv University, Tel Aviv, Israel; NIDDK, NIH, Bethesda,
3
MR; University of Washington, Seattle, WA
The M13 phage is a filamentous bacterial virus that consists
of thousands of identical coat protein subunits that wrap its
ssDNA genome. Using magic-angle spinning NMR
experimental data and Rosetta model building we generated a
structural model for the capsid of this micron-long particle.
The structure is best described by a series of symmetryrelated pentamers, where each pentamer represents five
identical coat protein subunits. We reveal the symmetry
ABSTRACTS OF TALKS
relating those pentamers, the diameter of the phage, the
structure of the individual subunits and their orientation with
respect to the viral axis. Overall, the capsid is stabilized by a
repeating hydrophobic/aromatic binding epitope that spirals
along the entire structure.
10:45 AM- 12:30 PM, TUESDAY MORNING
Conformational Dynamics and Allostery
Patrick Loria, presiding
Merrill Hall
TOB 10:45-11:10
Investigating the Role of Protein Mobility in
Interdomain Communication
1
1
2
Xingsheng Wang ; Jill Bouchard ; Junchao Xia ; Brendan
1
3
4
1
Mahoney ; John S. Zintsmaster ; David Case ; Jeffrey Peng
1
2
University of Notre Dame, Notre Dame, IN; Center for
Biophysics & Computational Biology, Philadelphia, PA;
3
4
Chevron Energy Tech. Co., Richmond, CA; Rutgers
University, Piscataway, NJ
Signaling proteins often rely on communication between
functional sites in different domains. A key step toward
understanding their signaling mechanisms is investigating
their mechanisms for interdomain communication. We have
carried such investigations for human Pin1, a two-domain
mitotic regulator that specifically recognizes phospho-Ser/ThrPro motifs in intrinsically disordered regions of other proteins.
This has involved using NMR measurements and molecular
dynamics simulations to compare the substrate-induced
changes in intra- and interdomain mobility for Pin1 and
several mutants. The different patterns of change suggest
dynamic allosteric regulation of the PPIase binding site, due to
substrate binding at the remote WW domain. Results and
implications for Pin1 recognition of disordered protein
segments will be discussed.
TOB 11:10-11:35
Solution NMR Techniques for the Characterization of
Chaperone–Substrate Complexes
Sebastian Hiller; Björn M. Burmann; Morgane Callon
Biozentrum, Basel, Switzerland
Protein folding in the cellular environment is often guided by
molecular chaperones. Due to the highly dynamic nature of
chaperone–substrate
complexes,
atomic
resolution
information on their structure and aggregation prevention
mechanisms is still very sparse. Here, we describe solution
NMR techniques to characterize chaperone–substrate
complexes. Importantly, the interpretation of NMR parameters
depends in a fundamental fashion on the shape of the
interaction energy landscape. For substrates that adopt
dynamic conformational ensembles, inter- and intramolecular
paramagnetic relaxation enhancements (PRE) determine the
compaction and localization. PRE-based substrate exchange
measurements determine the global complex lifetimes.
Intermolecular NOEs enable structural mapping of the direct
chaperone–substrate contact surface. We describe practical
examples, with a focus on periplasmic holdase chaperones
from outer membrane protein biogenesis.
TOB 11:35-12:00
Mapping Allosteric Networks through the Covariance and
Projection Analyses of NMR Chemical Shifts: Methods
and Applications
Giuseppe Melacini
Mcmaster University, Hamilton, Canada
The covariance and projection analyses of NMR chemical
shifts [1, 2] probe allosteric networks perturbed by a selected
set of covalent perturbations (e.g. a small focused library of
analogs of the endogenous allosteric effector and/or a group
of mutations). These methods have been particularly effective
in identifying otherwise elusive allosteric pathways, including
those underlying dynamically driven allosteric processes [1].
Here we show how the covariance and projection analyses of
chemical shifts can be used to map non-obvious allosteric
sites in dynamic linkers.
1. Selvaratnam R, Chowdhury S, VanSchouwen B & Melacini
G (2011) Proc Natl Acad Sci U S A 108: 6133-6138.
2. Selvaratnam R, VanSchouwen B, Fogolari F, MazhabJafari MT, Das R, Melacini G. (2012) Biophys J. 102 (3):6309.
TOB 12:00-12:15
Probing the Mechanism of Fibril Formation in D76N β-2Microglobulin with Ultra-Fast Magic-Angle Spinning
1
1
Tanguy Le Marchand ; Loren Andreas ; Emeline Barbet1
1
1
2
Massin ; Michael Knight ; Hugh Dannatt ; Stefano Ricagno ;
2
3
4
Martino Bolognesi ; Sofia Giorgetti ; Vittorio Bellotti ;
5
1
Lyndon Emsley ; Guido Pintacuda
1
2
Institut des Sciences Analytiques, Lyon, France; Department
3
of Biosciences, Milano, Italy; Department of Molecular
4
Medicine, Pavia, Italy; University College London, London,
5
UK; Ecole Polytechnique Federale de Lausanne,
Lausanne, Switzerland
Fibrils of a newly described D76N mutant of β2microglobulin
(β2m) were discovered as the causative agent in patients
suffering from gastrointestinal syndromes and autonomic
neuropathy.
Ultra-fast MAS on perdeuterated samples with full amide
1
reprotonation yields highly resolved H-detected correlations,
allowing resonance assignment of D76N β2m in
microcrystalline and fibril form.
We studied site-specific nano- to micro-second backbone
15
dynamics of microcrystalline D76N β2m by N relaxation and
REDOR experiments. A comparison with wild-type protein
highlights regions where the D76N mutant is particularly
destabilized, shedding light on the mechanism of formation of
the fibrils.
Chemical shift analysis of β2m fibrils shows the expected βstructure and homonuclear recoupling experiments revealed
1
1
long-range H- H contacts, indicating polymorphism occurring
under different growth conditions
TOB 12:15-12:30
F NMR Reveals Multiple Conformations at the Dimer
Interface of the Non-Structural Protein 1 Effector Domain
from Influenza A Virus
1
1
1
James Aramini ; Keith Hamilton ; Li-Chung Ma ; G.V.T.
1
2
2
3
Swapna ; Paul Leonard ; John Ladbury ; Robert Krug ;
1
Gaetano Montelione
1
2
CABM, Rutgers University, Piscataway, NJ; University of
3
Texas MD Anderson Center, Houston, TX; University of
Texas, Austin, TX
19
F NMR to NS1A from influenza
We have applied
A/Udorn/307/1972
virus
(H3N2)
labeled
with
519
fluorotryptophan (5-F-Trp), and demonstrate that the F
signal of Trp187 is a sensitive, direct monitor of the ED helix19
helix dimer interface. F relaxation dispersion data reveal the
19
Page 33
ABSTRACTS OF TALKS
presence of conformational dynamics within this functionally
important protein-protein interface, whose rate is over three
orders of magnitude faster than the kinetics of ED
19
dimerization determined by F saturation transfer difference
19
F NMR also affords direct spectroscopic
experiments.
evidence that Trp187, which mediates intermolecular ED:ED
interactions required for cooperative dsRNA binding, is
solvent exposed in full-length NS1A at subaggregate protein
concentrations. These results have important implications for
the diverse roles of this NS1A epitope during influenza virus
infection.
10:45 AM- 12:30 PM, TUESDAY MORNING
Metabolomics & Small Molecules
Yulan Wang, presiding
Chapel
TOC 10:45-11:10
Making NMR the Method of Choice in Metabolomics
David Wishart
University of Alberta, Edmonton, Canada
The advantages of using NMR for metabolomics are manifold.
It is non-destructive, non-biased, quantitative, requires no
separation and needs no chemical derivatization. However,
relative to other analytical techniques, NMR is slow and
insensitive. Furthermore the identification and quantification
of compounds in mixtures by NMR is manually intensive and
error-prone. Because of these limitations, NMR is being
supplanted by mass spectrometry for metabolomic
applications.
In this presentation I will describe new
instrumental and software techniques that my lab has
developed to perform rapid, automated NMR. I will further
show that when compared to other techniques, NMR is often
superior in terms of speed, sensitivity, coverage and its ability
to be automated.
TOC 11:10-11:35
Metabolomics and Drug Discovery
Robert Powers; Teklab Gebregiworgis; Steven Halouska;
Shulei Lei; Darrell Marshall; Emily Snell; Bradley Worley;
Bo Zhang
University of Nebraska-Lincoln, Lincoln, NE
Drug discovery is a complex and unpredictable endeavor with
a high failure rate. Consequently, a diseased-centered
systems biology approach provides a means to increase the
efficiency and success rate of drug discovery. One important
component of this approach is the use and development of
NMR and MS based metabolomics techniques to monitor the
in vivo activity and selectivity of potential drugs. Our
metabolomics
technology, including
our
MVAPACK
metabolomics software platform, PCA/PLS-DA utilities, and
protocols for integrating NMR and MS data, sample
preparation and metabolite identification will be discussed.
This presentation will include the application of our
methodology to pancreatic cancer, Parkinson’s disease,
Multiple Sclerosis and infectious diseases.
TOC 11:35-12:00
Defining Metabolomes: Roles of NMR and Challenges
Huiru Tang
Cas Key Lab Mr Biol Syst, Wuhan Inst Phys Math, Wuhan,
Phenomes represent all quantifiable features of a given
organism including macroscopic and molecular phenomes
which result from interactions of genomes and environmental
factors. Metabolomes are essential parts of molecular
Page 34
phenomic features and important aspects of an integrated
biological system and its functioning. Rich quantitative,
topographical and molecular information for metabotypes give
NMR technologies vital roles in defining metabolomes
(molecular phenotyping) and understanding cellular, tissue
and whole organism systems. The huge diversity of
metabolites in complex biological systems, makes
metabolomics technologies in demand even though a
framework of metabonomic analysis has been developed
during last decade. Our presentation deals with the needs,
bottlenecks and possible future strategies in the field of
quantitative metabonomics and dynamic metabolism for
magnetic resonance techniques.
TOC 12:00-12:15
Ultrafast Double-Quantum NMR Spectroscopy
1
2
2
Adrien Le Guennec ; Laetitia Rouger ; Boris Gouilleux ; Ilya
3
3
1
Kuprov ; Malcolm Levitt ; Stefano Caldarelli ;
2
1
Patrick Giraudeau ; Jean-Nicolas Dumez
1
2
ICSN - CNRS, Gif-Sur-Yvette, France; Université de Nantes,
Nantes Cedex 03, N/A;
3
Southampton University, Southampton
We show that double-quantum NMR spectra (DQS)
can be recorded in less than 3 seconds with ultrafast NMR
(UF) and that they provide significant improvements in
spectrum quality over classic sequences. We illustrate the
potential of UFDQS for the analysis of complex mixtures, on
the example of a model mixture of metabolites. These
experiments exploit the strong synergies between ultrafast
NMR and double-quantum NMR.
We also describe and use a general and efficient
platform for the simulation of spatially encoded experiments.
The complex spin dynamics underlying the spatial encoding of
multiple-quantum coherences are best analysed with the
support of numerical simulations. Beyond UFDQS, this joint
description of the space and spin variable can be useful for a
variety of experiments.
TOC 12:15-12:30
HOBS: Broadband Homonuclear Decoupled BandSelective NMR Experiments with full sensitivity
Laura Castañar Acedo; Albert Vigili; Teodor Parella
Universitat Autónoma Barcelona, Cerdanyola Del Vallés,
Barcelona, Spain
Recently, a novel NMR approach for recording broadband
HOmodecoupled Band-Selective (HOBS) NMR spectra with
full sensitivity has been reported.The HOBS technique is a
frequency-selective
experiment
which
affords
fully
homodecoupled singlet signals in particular areas of the 1H
spectrum without sacrificing sensitivity, allowing the fast NMR
data acquisition in the same experimental times as regular
experiments. Here we present the easy and reliable
implementation of the HOBS technique for a number of homoand heteronuclear multidimensional experiments, such as
HOBS-TOCSY, HOBS-HSQC, HOBS-HSQMBC, HOBSInversion-Recovery and HOBS-CPMG-PROJECT. In addition,
its practical utility in a wide range of applications, covering the
n
direct measurement of JCH, the determination of T1 and T2
NMR relaxation times and the enantiodifferentiation studies,
among other.
ABSTRACTS OF TALKS
4:00 – 5:50 PM, TUESDAY AFTERNOON
NMR and Computation in Structure Calculation
Rafael Bruschweiler, presiding
Merrill Hall
proteins, fast-folding proteins, weakly structured peptides, and
disordered proteins, we are further optimizing force fields to
more accurately simulate proteins across the order-to-disorder
spectrum.
TOD 4:00-4:25
Bayesian Inference for Biomolecular
Structure Determination
1, 2
Michael Habeck
1
2
University of Göttingen, Göttingen, Germany; Max Planck
Institute for Biophysical Chemistry, Göttingen, Germany
The Inferential Structure Determination (ISD) approach views
biomolecular structure determination as an inference problem
that should be solved by applying Bayesian probability theory.
I will give a short background on ISD and use recent NMR
structure determinations to illustrate the strengths of the
approach. I will discuss algorithmic improvements based on
concepts from statistical mechanics and outline how these
can be used to compare alternative models. Bayesian model
comparison allows one to compare quantitatively, in the light
of the given data, different force fields, restraint potentials, or
oligomeric states. Finally, I will outline how to infer entire
conformational ensembles rather than single structures from
ensemble-averaged data using the ISD framework.
TOD 5:05-5:20
Advances in Modeling the Structures of Biomolecular
Assemblies from NMR and Cryo-EM Data
1
5
4
Nikolaos Sgourakis ; Jean-Philippe Demers ; Omry Morag ;
6
3
3
Birgit Habenstein ; Antoine Loquet ; Suresh Kumar Vasa ;
3
4
3
2
Stefan Becker ; Amir Goldbourt ; Adam Lange ; David Baker
1
2
NIDDK, NIH, Bethesda, MD; University of Washington,
3
4
Seattle, WA; Max Planck Institute, Goettingen, Germany; Tel
5
Aviv University, Tel Aviv, N/A; Max-Planck Institute BPC,
6
Göttingen, Germany; Institut de Biologie et Chimie des
Proteines, Lyon, France
We introduce a general hybrid approach for determining the
structures of supramolecular assemblies. Cryo-electron
microscopy and X-ray fiber diffraction data define the overall
envelope of the assembly, symmetry parameters and rigidbody orientation of the subunits while magic-angle spinning
solid-state NMR chemical shifts and distance constraints
define the local secondary structure, protein fold and intersubunit interactions. Finally, Rosetta “fold-and-dock” structure
calculations provide a general framework to integrate the
different sources of structural information. We illustrate the
application of the new approach for two key systems. A) The
type-III secretion system needle of Shigella flexneri. B) The
intact M13 filamentous phage capsid. Our results demonstrate
the strength of the hybrid approach as a method of choice to
study
noncrystalline,
high-molecular-weight
molecular
assemblies.
TOD 4:25-4:50
Hybrid Approaches for Protein Structure Determination
Combining Computational Modeling with
Sparse NMR Restraints
Gaetano Montelione
Rutgers University, Piscataway, NJ
We have developed a hybrid approach that uses evolutionary
couplings from the sequence record together with sparse
NMR data to determine accurate 3D protein structures. We
demonstrate this hybrid “EC-NMR” method by determining
accurate structures of proteins ranging in size from 6 to 40
kDa. We have also explored generation and refinement of
protein NMR structures using Rosetta with experimental NMR
restraints. Restrained CS-Rosetta has also been used to
determine NMR structures for proteins up to 40 kDa, utilizing
sparse distance restraints, RDCs, and chemical shift data
obtained on perdeuterated samples. These hybrid
computational methods should be broadly useful extending
the range of protein structures which can be determined using
NMR data.
TOD 4:50-5:05
Developing Force Fields for the Accurate Simulation of
Both Ordered and Disordered Protein States
1
1
1
Paul Robustelli ; Stefano Piana ; Alexander Donchev ; David
1, 2
Shaw
1
2
D.E. Shaw Research, New York, New York; Columbia
University, New York, New York
We present an extensive benchmark study to systematically
assess the ability of commonly used molecular dynamics
force fields to reproduce NMR, SAXS, and FRET data for a
number of ordered and disordered proteins. We found that,
while the properties of folded proteins are generally well
described in simulation, large discrepancies exist between
simulation and experiment for disordered proteins. We
developed a new water model that better balances
electrostatic and dispersion interactions, resulting in
significantly improved accuracy in the description of
disordered states, but slightly degraded results for ordered
proteins. Guided by experimental measurements from folded
TOD 5:20-5:35
Probing the Structural and Dynamical Effects of the
Charged Residues of the TZF Domain of TIS11d
Brittany Morgan; Laura Deveau; Francesca Massi
University of Massachusetts, Worcester, MA
CCCH-type tandem zinc finger (TZF) domains are found in
many proteins that bind RNA and specifically regulate posttranscriptional gene expression. In the TZF domain of TIS11d
the C-terminal residue E220 is important in stabilizing a
compact structure in the absence of RNA. To investigate how
E220 stabilizes the structure of TIS11d, the mutants TIS11dE220A and TIS11d-ΔD219/E220 (where D219 and E220 were
deleted) were studied using molecular dynamics and validated
with NMR spectroscopy. We observed a greater structural
heterogeneity for both mutant proteins than in the wild type.
From these results and patterns of evolutionary conservation
in related protein sequences, we posit that favorable
electrostatic interactions provide a mechanism to promote
preferential orientation of the zinc fingers without imposing
structural rigidity.
TOD 5:35-5:50
A Statistical Torsion Angle Potential Improves the Quality
of NMR-based RNA Structures
Guillermo Bermejo; Marius Clore; Charles Schwieters
National Institutes of Health, Bethesda, MD
A growing consensus among structural biologists suggests
that the backbone of RNA is rotameric, i.e, only a finite
number of discrete backbone conformers are physically
allowed. Upon surveying structures from the Protein Data
Bank we found that NMR-based RNA structures contain, in
general, a larger fraction of conformational outliers than high-
Page 35
ABSTRACTS OF TALKS
resolution X-ray counterparts. Here, we develop a new
statistical torsion angle potential for RNA by applying adaptive
kernel density estimation on a database of high-resolution Xray structures. When tested on a set of six RNA systems, we
find that the statistical potential, implemented during
molecular dynamics calculations, reduces the fraction of
backbone conformational outliers and improves the
agreement with cross-validated residual dipolar couplings.
4:00 – 5:50 PM, TUESDAY AFTERNOON
Novel MRI Applications
Adrian Carpenter, presiding
Chapel
TOE 4:00-4:25
Translational Imaging of Fat Metabolism
S. Sendhil Velan
Singapore Bioimaging Consortium, Singapore
The study of fat distribution is important to understand the
pathophysiology of obesity-related disorders, diabetes mellitus
and cardiovascular diseases. Magnetic Resonance Imaging
and Spectroscopic techniques permit longitudinal assessment
of metabolic changes. In this talk I will share some of our
findings with pre-clinical and clinical metabolic investigations.
We investigated the developmental and genetic pathways to
metabolic diseases through the Singapore Adults Metabolism
Study (SAMS). In this study, we studied the influence of
ethnicity in contributing to the risk of obesity and diabetes in
the Asian population. We determined the body’s distribution of
fat and its functional relationship to other insulin-sensitive
sites such as the skeletal muscle, liver and abdominal adipose
tissues in a multiethnic cohort of normal and overweight
adults.
TOE 4:25-4:50
Metabolic and Molecular Imaging by
Hyperpolarized Magnetic Resonance
Arnaud Comment
Ecole Polytechnique Fédérale de Lausanne,
Lausanne, Switzerland
Hyperpolarization by dissolution dynamic nuclear polarization
(DNP) increases the sensitivity of X-nuclei magnetic
resonance (MR) by several orders of magnitude offering the
opportunity to perform real-time in vivo MR spectroscopy and
imaging experiments. It becomes possible to follow the
kinetics of a variety of novel contrast agents and probe fast
biochemical transformations from labeled precursors to
metabolic products in vivo. Using a unique setup for in vivo
hyperpolarized MR, we show that it is possible to perform
experiments with a large variety of agents. Some examples of
in vivo metabolic and molecular imaging performed in rodents
will be given to illustrate the potential of these methods for
biomedical applications and illustrate the importance of
reproducible and automated protocols.
TOE 4:50-5:05
13
High Resolution 3D Hyperpolarized C Imaging
Techniques
1
1
2
Eugene Milshteyn ; Cornelius von Morze ; Galen Reed ;
1
1
1
1
Hong Shang ; Peter Shin ; Zihan Zhu ; John Kurhanewicz ;
1
1
Robert Bok ; Daniel Vigneron
1
2
UCSF, San Francisco, California; Heartvista,
Menlo Park, CA
13
The development of hyperpolarized (HP) C imaging has
enabled noninvasive metabolic imaging with magnetic
Page 36
13
resonance imaging. The use of HP C is particularly powerful
in vivo because of the capability to study multiple metabolic
pathways and physiology, such as perfusion, simultaneously
in real time. Here, we developed a specialized high resolution
3D sequence that provided 1.5 mm isotropic images of [113
13
13
15
C]lactate, [1- C]pyruvate, and [ C, N2]urea in normal rats
and mice with transgenic breast and prostate tumors. The
improved spatial resolution of the images indicates the value
of this approach for clinical imaging.
TOE 5:05-5:20
Dynamic in vivo Free Radical Imaging with OverhauserEnhanced MRI
1, 2
3
1, 2
Mathieu Sarracanie ; Fanny Herisson ; Najat Salameh ;
1, 4
3, 5
1, 5
David Waddington ; Cenk Ayata ; Matthew Rosen
1
MGH/A.A. Martinos Center for Biomedical Imaging,
2
Charlestown, MA; Department of Physics, Harvard
3
University, Cambridge, MA; Neurovascular Research Lab,
4
MGH, Charlestown, MA; School of Physics, University of
Sydney, Sydney, Australia;
5
Harvard Medical School, Boston, MA
We explore here the use of b-SSFP based OMRI to acquire
free radical images with sufficient spatial and temporal
resolution to probe oxidative stress status via free radical
decay dynamics in the rat brain. We present here timeresolved OMRI following a single injection of TEMPOL in
healthy living rats. Sixteen full 11 slice OMRI data sets were
acquired over 240 seconds at 6.5 mT. Free radical contrast is
clearly seen in the hemisphere ipsilateral to the injection. The
results presented here suggest that temporally resolved OMRI
in conjunction with an exogenous free radical agent may allow
study the redox status of brain tissue.
TOE 5:20-5:35
An Optimal Pulse for Fluid-Suppressed Sodium
Knee MRI at 7 T
Jae-Seung Lee; Ding Xia; Ravinder Regatte
Department of Radiology, New York University, New York, NY
23
In the field of Na MRI, inversion recovery (IR) has been a
popular method to discriminate the sodium content between
different environments. For example, IR can be used to
suppress the signal from surrounding synovial fluid in the
knee joint, so the sensitivity for the sodium content within
cartilage can be improved. For the more efficient inversion
under B0 and B1 inhomogeneities, adiabatic inversion pulses,
such as the WURST pulses, are usually employed. In this
work, we numerically produced an RF shape to substitute for
the adiabatic inversion pulse in the IR sequence, which may
23
improve the performance of Na fluid-suppressed knee MRI
in terms of efficient fluid suppression, improved contrast
between cartilage and artery, and reduced specific absorption
rate.
TOE 5:35-5:50
Group Sparse Reconstruction of Highly Undersampled
Echo Planar Correlated Spectroscopic Imaging Scan:
Application to Human Calf
Neil Wilson; Brian Burns; Zohaib Iqbal; M. Albert Thomas
UCLA, Los Angeles, CA
Acquiring a five dimensional MR-spectroscopic imaging scan
(3 spatial and 2 spectral dimensions) is impractical due to very
long scan times. However, by incorporating an echo planar
readout to encode one spectral and one spatial dimension
simultaneously and reconstruction using compressed sensing,
this nonuniform sampling based acquisition opens up a
ABSTRACTS OF TALKS
possibility to be performed in a clinically feasible scan time. In
this work, we propose a novel reconstruction method that
groups nearby data points (Group Sparsity). We evaluated
this method on a 3T MRI scanner using a single channel
transmit/receive extremity coil. Multi-voxel correlated spectra
were recorded in human calf muscle in vivo. The new
reconstruction method performed better than a comparison
CS reconstruction method, as demonstrated in several voxels.
8:30 – 10:15 AM, WEDNESDAY MORNING
Electron Meets Nucleus
Song-I Han, presiding
Merrill Hall
WOA 8:30-8:55
Dynamic Nuclear Polarization with Endogenous
Polarizing Agents
Björn Corzilius
Goethe University, Frankfurt Am Main, Germany
Direct DNP of biomolecules with endogenous paramagnetic
metals as polarizing agents is a promising technique for
structural biology investigations. In this presentation the
chemical and spectroscopic properties of suitable metal ions
2+
3+
(i.e., Mn , Gd ) are reviewed and several routes for the
labeling of biomolecules with paramagnetic metals will be
discussed. Several biomolecular systems containing
paramagnetic metal ions including proteins and nucleic acids
will be presented. We show EPR and MAS NMR experiments
in order to investigate metal binding, electron spin properties,
as well as electron–nuclear interactions such as paramagnetic
relaxation and signal quenching. Finally we will demonstrate
13
the direct, intramolecular DNP of C from endogenous metal
sites in biomolecules.
WOA 8:55-9:20
Recent Insights in Overhauser DNP at 0.3 and 3 Tesla
Marina Bennati
MPI for Biophysical Chemistry, Göttingen, Germany
We have been investigating the mechanism of Overhauser
DNP at two different polarizing fields, 0.3 and 3 Tesla, in
conjunction with nitroxide radicals polarizers. At 0.3 Tesla,
liquid DNP to water protons has led to the observation of high
enhancements that almost reach the theoretical limit. The
availability of pulse electron spin resonance gave insight into
the role of electron spin saturation and field dependence of
the coupling factor. This talk will present our approaches to
obtain a quantitative picture of the Overhauser enhancements
and will discuss possible strategies to achieve large
enhancements in high resolution NMR at high fields.
Furthermore we present an experiment to polarize nuclei with
large and weak hyperfine couplings via pulsed electron and
nuclear excitation.
WOA 9:20-9:45
Dynamic Nuclear Polarization (DNP) with MAS for
Biomolecular Solid-State NMR
Kent Thurber; Wai-Ming Yau; Robert Tycko
National Institutes of Health, Bethesda, MD
I will discuss recent results on biomolecular solid-state MASNMR using DNP at low temperatures (~25 K). DNP increases
the NMR signal by transferring polarization from unpaired
electrons to nuclei. One part of our current work is preparing
samples for solid-state DNP-NMR by rapid mixing and
freezing of solutions of biomolecules. Our low-temperature
DNP-MAS-NMR experiments use a home-built probe typically
at ~25 K and ~7 kHz MAS at 9.4 Tesla. The microwaves for
electron spin saturation are provided by an Extended
Interaction Oscillator (EIO) (up to 1.4 W at 264 GHz). For a
sample at 24 K (of the peptide melittin frozen in water/glycerol
doped with 10 mM of a tri-nitroxide molecule), saturation of
the DNP occurs at roughly 1 W.
WOA 9:45-10:00
Local and Bulk 13C Hyperpolarization in NV-Centered
Diamonds at Variable Fields and Orientations
1
1
Gonzalo Agustin Alvarez ; Christian Oliver Bretschneider ;
2
2
3
4
Ran Fischer ; Paz London ; Hisao Kanda ; Shinobu Onoda ;
5
2
1
Junichi Isoya ; David Gershoni ; Lucio Frydman
1
2
Weizmann Institute of Science, Rehovot, Israel; Technion,
3
Haifa, Israel; National Institute for Materials Science,
4
Tsukuba, Japan; Japan Atomic Energy Agency, Takasaki,
5
Japan; University of Tsukuba, Tsukuba, Japan
Polarizing nuclear spins is of importance in biology, chemistry
and physics. Methods for hyperpolarizing 13C-nuclei from free
electrons in bulk, demand operation at cryogenic
temperatures. Room-temperature approaches targeting
diamonds with nitrogen-vacancy centers alleviate this need
exploiting level anti-crossings that allow the exchanging of
polarization from fully polarized electrons to the nuclei. This
method requires suitable conditions on the strength and
alignment of the magnetic field. To make the approach
versatile, we developed a different method for achieving
electron→13C spin-alignment transfers on a broad range of
magnetic field strengths and orientations. This versatility
results from combining microwave- and laser-induced
transitions between selected energy-states of the coupled
electron-nuclear
spin-manifold.
13C-detected
NMR
demonstrates that this hyperpolarization can be transferred
throughout the nuclear bulk-ensemble.
WOA 10:00-10:15
Room-Temperature in situ Nuclear Spin Hyperpolarization
from Optically-Pumped Nitrogen Vacancy
Centers in Diamond
1, 2
1, 2
Jonathan P King ; Keunhong Jeong ; Christophoros
1, 2
1, 2
1
1, 2
Vassiliou ; Chang Shin ; Ralph Page ; Claudia Avalos ;
1
1, 2
Haijing Wang ; Alex Pines
1
Department of Chemistry, UC Berkeley, Berkeley, CA;
2
Materials Sciences Division, LBNL, Berkeley, CA
13
We report bulk, room-temperature hyperpolarization of C
nuclear spins observed via high-field NMR. Hyperpolarization
is achieved by optical pumping of nitrogen vacancy (NV )
defect centers in diamond accompanied by dynamic nuclear
polarization (DNP). This technique harnesses the large
−
optically-induced spin polarization of NV centers at room
temperature. The optical pumping/DNP is performed at 420
mT, where inductive detection of NMR is feasible. Here, we
report bulk nuclear spin polarization of 6%. This polarization is
generated in situ and detected with a standard, inductive NMR
probe without the need for sample shuttling or precise crystal
orientation. Hyperpolarization via OP/DNP should operate at
arbitrary magnetic fields, enabling orders of magnitude
sensitivity enhancement for NMR of solids and liquids at
ambient conditions.
Page 37
ABSTRACTS OF TALKS
10:45 AM – 12:30 PM, WEDNESDAY MORNING
Bioliquids
Wolfgang Jahnke, presiding
Merrill Hall
WOB 10:45-11:10
Kinetics Matter: Elucidation the Mechanism of
Transcriptional Riboswitches by NMR
Harald Schwalbe
Univ of Frankfurt, Frankfurt, Germany
Riboswitches are gene regulatory elements located in the 5’untranslated regions of messenger RNA (mRNA). Ligand
binding to an aptamer domain of riboswitches induces either
the up- or down-regulation of the expression of ligandassociated genes. Riboswitch regulate gene expression either
at the level of transcription or translation. For transcriptional
riboswitches, ligand binding supposedly induces a
conformational
switch
between
mutually
exclusive
antiterminator or terminator conformations that represent the
on- and off-states of the switches.
WOB 11:10-11:35
13
New Methods Based on C Direct Detection to Study
Intrinsically Disordered Proteins
Isabella C. Felli
CERM University of Florence, Sesto Fiorentino
(Florence), Italy
The growing interest in understanding the functional role of
protein intrinsic disorder and flexibility, has stimulated the
development of new NMR methods to study intrinsically
disordered proteins (IDPs). The high flexibility and largely
solvent exposed backbone of IDPs influence NMR parameters
causing reduced chemical shift dispersion and extensive
broadening of amide proton resonances, in particular
13
C detected NMR
approaching physiological conditions.
experiments now offer a valuable tool to address these
peculiar features of IDPs. The experimental variants to
13
improve the performance of C detected NMR experiments to
study IDPs will be discussed. These open the way to the
characterization of IDPs of increasing size and complexity and
to in-cell studies. Several examples will be presented.
WOB 11:35-12:00
Testing the Multidrug Transport Mechanism of EmrE
1
1
1
Emma Morrison ; Supratik Dutta ; Anne Robinson ; Greg
1
1
1, 2
Dekoster ; Chao Wu ; Katherine Wildman
1
2
Washington University, Saint Louis, MO; University of
Wisconsin, Madison, WI
EmrE is a small multidrug resistance transporter that exports
a broad class of polyaromatic cation substrates from E. coli.
We have established the functional importance of
conformational exchange between open-in and open-out
states using chemical cross-linking to block this step in the
transport cycle both in vitro and in vivo. Exploiting the natural
toolkit provided by diverse EmrE substrates, we have used to
NMR to determine that the rate of this key conformational
exchange process is determined by the transported substrate.
Using NMR-based pH titrations, we now find that coupling of
drug export to proton import is more complex than proposed
in the original single-site alternating access model.
WOB 12:00-12:15
Transient Complexes Observed by Paramagnetic
Ntr
Relaxation Enhancement between Enzyme 1 and NPr
Prevent Crossover between Phosphorylation Pathways
Page 38
1
2
Madeleine Strickland ; Ann Marie Stanley ; Guangshun
3
4
1
1
Wang ; Susan Buchanan ; Alan Peterkofsky ; Nico Tjandra
1
2
NHLBI, NIH, Bethesda, MD; NIGMS, NIH, Bethesda, MD;
3
Nebraska Medical Center, Omaha, NE;
4
NIDDK, NIH, Bethesda, MD
Ntr
Enzyme I and NPr are the first two enzymes in a recently
characterized phosphoryl transfer pathway paralogous to the
PTS
(phosphoenolpyruvate:sugar
phosphotransferase)
system. However, the relatively large size of the 38 kDa
Ntr
Ntr
enzyme I N-terminus:NPr complex (EIN :NPr) limits the
number of conventional NMR restraints that can be measured.
Ntr
Using the crystal structure of EIN and the NMR structure of
NPr, both in the free form, we acquired residual dipolar
couplings (RDCs) and paramagnetic relaxation enhancement
(PRE) data in order to investigate the structure of the complex
and transient encounter complexes, respectively. We found a
simple, elegant mechanism involving transient complexes that
prevents crossover between the two paralogous pathways.
WOB 12:15-12:30
NMR to Measure Molecular-Level Curvature of
Membranes by Proteins and Lipids
Adrian Draney; Sean Smrt; Justin Lorieau
U Illinois, Chicago, Chicago, IL
The bending and curvature of biological membranes is tightly
regulated by cells and involved in processes as diverse as the
transmission of neurotransmitters, the formation of vesicles,
cellular endocytosis and viral infection. We investigate how
NMR can be used to measure membrane curvature from only
a few foreign lipid or protein molecules. Our approach uses
bicelle induced curvature and sorting (BICS) with isotropicallytumbling bicelles to study minute changes in bicelle sizes and
dynamics by foreign lipids and protein molecules. We show
that BICS is a powerful experiment for quantitatively
measuring molecular-level membrane curvature with the
sensitivity of detecting changes in membrane structure and
dynamics from a few perturbing lipids. These experiments are
extended to study the curvature function of proteins.
10:45 AM – 12:30 PM, WEDNESDAY MORNING
Exotica
Sophia Hayes, presiding
Chapel
WOC 10:45-11:10
Ultra-Precise NMR-Magnetometers for High Fields
Peter Bluemler; Anna Nikiel; Andreas Maul; Sergei Karpuk;
Ernst Wilhelm Otten; Werner Heil
Institute of Physics, Mainz, Germany
A magnetometer for extremely precise measurements of high
3
magnetic fields is presented. It uses a few mbar of He in
perfectly spherical quartz cells (ID=8mm). The low pressure
assures motionally narrowed NMR signals with very long
coherence times T2*, which are needed to achieve the desired
-13
3
precision (10 ). Due to the small number of spins the He
has to be hyperpolarized to give a useful NMR-signal, for
which a special variant of metastability optical pumping had to
be developed. With our current setup we observed a T2* of
-12
200 s at 1.5 T giving a precision of 10 which is sufficient for
high precision mass-spectroscopy using Penning traps to test
for the standard model of physics.
ABSTRACTS OF TALKS
WOC 11:10-11:35
What NMR Can Tell Us About Metal Organic Frameworks
Jeffrey Reimer
UC Berkeley, Berkeley, CA
Modern magnetic resonance methods inform researchers
about local bonding configurations, the distribution of bonding
environments at the nanoscale, and the dynamics of
molecules. I will illustrate these three outcomes of NMR,
respectively, by describing how adsorbates chemically react
with functionalized MOFs, how linkers are apportioned within
multivariate MOFs, and how the motion of solvent molecules
yield pore sizes and phase behavior in a variety of MOFs.
WOC 11:35-12:00
Synchronous Hyperpolarization and NMR of Xe Gas
Thad Walker; Anna Korver; Daniel Thrasher;
Michael Bulatowicz
Univ. of Wisconsin-Madison, Madison, Wisconsin
Hyperpolarized Xe gas is produced by spin-exchange
collisions with optically spin-polarized Rb atoms. The Rb
atoms form an embedded ultra sensitive magnetometer for
detecting the Xe NMR, with a 500x quantum enhancement of
the Xe NMR signals. Such a system holds promise for subnHz scale frequency resolution, were it not for a large NMR
frequency shift due to the polarized Rb atoms. To mitigate
this, we make the Rb and Xe spins synchronously precess in
a plane transverse to the NMR bias field. To allow this to
happen despite the 1000x ratio of Rb to Xe gyromagnetic
ratios, we replace the usual DC bias field by a sequence of
carefully spaced short pulses.
WOC 12:00-12:15
Phosphorus-31 MRI of Hard and Soft Solids using
Quadratic Echo Line-Narrowing
Sean Barrett
Yale University Physics Dept., New Haven, CT
Magnetic resonance imaging (MRI) of solids is challenging.
One reason is that the broader MR linewidths, compared to
the narrow resonance of water, limit both the attainable spatial
resolution and the signal-to-noise ratio. Basic physics
research, stimulated by the quest to build a quantum
computer, unexpectedly gave rise to a “quadratic echo” pulse
sequence, which can narrow the broad MR spectrum of
solids. Applying field gradients in sync with this line-narrowing
sequence offers a fresh approach to the MRI of hard and soft
solids with high spatial resolution and with a wide range of
potential uses. For example, this method can be used to carry
out three-dimensional MRI of the phosphorus (31P) in ex vivo
bone and soft tissue samples.
WOC 12:15-12:30
The Principle of Reciprocity in Conductors
1, 2
1
2
Andrew Ilott ; Mohaddese Mohammadi ; Hee Jung Chang ;
3
3
1
Nicole M. Trease ; Clare P. Grey ; Alexej Jerschow
1
2
New York University, New York, NY; Stony Brook University,
3
Stony Brook, NY; University of Cambridge, Cambridge, UK
The effect of the principle of reciprocity on the NMR signal of
metals is explored. It is demonstrated that the nutation curve
of a bulk metal is particularly sensitive to the details of
reciprocity. This is due to the form of the complex rf field that
is attenuated by the skin effect at the surface of the conductor,
and means that both the positively and negatively rotating
frames must be accounted for in the analysis. These effects
can be exploited to probe slow exchange and self-diffusion in
metals, and to ascertain the distribution of nuclei over
distances comparable to the skin depth.
4:00 – 6:00 PM, WEDNESDAY AFTERNOON
Tutorial Session
Albert Thomas, presiding
Merrill Hall
These presentations and slides will be recorded and posted to
the ENC web site.
WOD 4:00-4:40
Using Solution State NMR to Understand the
Conformational Behavior of Intrinsically Disordered
Proteins; Martin Blackledge
IBS Grenoble
WOD 4:40-5:20
You Spin Me Right Round: Tensors and Rotations in NMR
Leonard Mueller
University of California, Riverside
WOD 5:20-6:00
Insights into Ultra High-Field NMR Magnet Technology
Gerhard Roth
Bruker BioSpin GmbH
8:30 – 10:05 AM, THURSDAY MORNING
Methods Development in MRI
Daniel Vigneron, presiding
Merrill Hall
ThOA 8:30-8:55
Frequency- and Gradient-Modulated MRI: Imaging with
Extreme Field Inhomogeneity
Michael Garwood; Albert Jang; Naoharu Kobayashi;
Sung-Min Sohn; Thomas Vaughan
University of Minnesota, Minneapolis, MN
Fourier-based imaging offers limited ability to produce clinicalquality images of humans using small, portable magnets that
produce extremely inhomogeneous B0. Improved tolerance to
B0 inhomogeneity with spatiotemporal-encoded MRI has been
demonstrated, but these improvements were limited because
B0 compensation was restricted to one or possibly two spatial
directions simultaneously. Now, due to the invention of 3D
frequency-swept excitation pulses in a technique we call
STEREO, it should be possible to compensate for extreme B0
inhomogeneity and thus accomplish MR imaging of humans
using small, portable magnets. STEREO, which stands for
steering resonance over the object, produces images by
moving a localized resonant region along a curved spatial
trajectory such that excitation itself is spatially selective and
temporally sequential.
ThOA 8:55-9:20
New Directions for Brain MRI Hardware and Acquisition
1, 2
Lawrence L. Wald
1
2
MGH Martinos Center, Charlestown, MA; Harvard-MIT
Division of Health Sciences and Tech., Cambridge, MA
This talk will discuss our work on new hardware methods to
widen the space within which MRI may be applied. This
includes improving sensitivity and encoding with highly
parallel RF coils and coupling them to B0 shimming. We look
to improve MR’s molecular imaging by coupling acoustic
waves and MR contrast generation around iron oxide nanoparticles to turn the agent’s contrast effect “on” and “off.”
Finally, we note that the weight, power and cooling
Page 39
ABSTRACTS OF TALKS
requirements are barriers to bringing MRI to the patients. We
have developed a portable brain MRI system (<100 kg) which
does not use traditional gradient coils at all, but encodes brain
images by rotating an inhomogeneous magnet around the
patient’s head.
ThOA 9:20-9:35
A Robust Suite of Fast and Ultrafast Methods for In Vivo
Spectroscopy Imaging of pre-Targeted Metabolic Peaks
1
1, 2
1, 3
Amir Seginer ; Zhiyong Zhang ; Noam Shemesh ; Rita
1, 4
1
Schmidt ; Lucio Frydman
1
2
Weizmann Institute, Rehovot, Israel; Xiamen University,
3
Xiamen, China; Champalimaud Centre for the Unknown,
4
Lisbon, Portugal; Leiden University Medical Center, Leiden,
The Netherlands
We present a series of fast and ultrafast (single shot) robust
sequences, for in vivo spectroscopic imaging. Speed in these
2D/1D spatial/spectral experiments is achieved by addressing
only user-selected, pre-determined resonances. These are
efficiently encoded by relying on either polychromatic
selective pulses, or on spatiotemporal encoding pulses such
as those used in ultrafast 2D NMR. Robustness is achieved
by endowing the sequences with spin-echo or spatiotemporalecho characters, thus eliminating T2* effects. The ensuing
SPatiotemporal ENcoded Spectroscopic Imaging (SPENSI),
PolyChromatic SPatiotemporal Encoding (PC-SPEN), and
Relaxation
Enhanced
Chemical
shift-Encoded
Spectroscopically-Separated (RECESS) sequences, will be
described and their in vitro and in vivo performances
evaluated.
ThOA 9:30-9:50
Isolated Amide Proton CEST Contrast at 7 T Correlates
with Contrast-Enhanced T1w-Images of Tumor Patients
1
1
1
Johannes Windschuh ; Steffen Goerke ; Jan-Eric Meissner ;
2
1
1
Alexander Radbruch ; Peter Bachert ; Moritz Zaiss
1
German Cancer Research Center, Heidelberg, Germany;
2
University of Heidelberg Medical Center,
Heidelberg, Germany
The in vivo CEST signal of amide protons (Δω = 3.5 ppm from
the free water resonance) is contaminated by an underlying
aromatic nuclear Overhauser effect (NOE). By assuming a
constant ratio between aromatic and aliphatic NOE the
exchange-dependent amide proton signal can by isolated,
leading to a contrast that is solely dependent on pH and
amide proton concentration. This was confirmed by studies in
aqueous bovine serum albumin (BSA) solution on a 14.1-T
NMR spectrometer and applied to CEST images of 12
patients with newly diagnosed glioblastoma at 7 T.
Remarkably, the resulting isolated amide proton contrast
correlates strongly with the tumor ring enhancement resolved
in gadolinium enhanced T1-weighted images.
ThOA 9:50-10:05
Magnetic Resonance Imaging of Metabolically Labeled
Glycans using Hyper-CEST Xenon Biosensors in a
Live-Cell Bioreactor
Christopher Witte; Honor Rose; Vera Martos Riaño; Stefan
Reinke; Stefan Klippel; Christian Hackenberger; Leif Schröder
Leibniz-Institut für Molekulare Pharmakologie,
Berlin, Germany
Recent work demonstrated the first MRI of molecular targets
using saturation transfer with xenon biosensors in cellulo,
though the question remains if xenon biosensors can address
targets that have proven challenging for proton MRI. An ideal
Page 40
case study to address this question is molecular imaging of
metabolically-labelled cell-surface glycans, as successful MRI
of conventional contrasts agents targetted to such glycans
remains elusive. We designed a multimodal xenon
MRI/fluorescence biosensor targeted to metabolically labeled
sialic acid through bioorthogonal chemistry. The specificity of
the biosensor was confirmed using flow cytometry and
fluorescence microscopy. Using our custom NMR-compatible
live-cell bioreactor we demonstrate that Hyper-CEST xenon
biosensors can successfully image the distribution of
metabolically-labelled cell-surface glycans in cellulo at
nanomolar concentrations.
10:45 AM – 12:35 PM, THURSDAY MORNING
DNP: Methods and Applications
Melanie Rosay, presiding
Merrill Hall
ThOB 10:45-11:10
Mechanistic Studies of Dynamic Nuclear Polarization
Joanna R. Long
University of Florida, Gainesville, FL
I will describe efforts at the U.S. National High Magnetic Field
Laboratory to develop a DNP user facility with unique
capabilities for mechanistic DNP studies. This facility
encompasses three separate DNP approaches: 1) DNPenhanced MAS ssNMR at 14.1 T and 100 K for solids
applications; 2) DNP at 5 T and 1.1 K for in vivo metabolism
applications and 3) Overhauser DNP at 14.1 T and ambient
temperature for small molecule applications. My talk will focus
in particular on our use of a quasioptical table for gating of
microwaves within the MAS ssNMR experiments and various
samples preparation strategies for membrane protein
samples.
ThOB 11:10-11:35
Dissolution DNP: Hardware and Methodology
Fabian Jähnig; Marcin Krajewski; Michael Batel; Sebastian
Kozerke; Matthias Ernst
ETH Zurich, Zurich, Switzerland
Hardware and methodological developments to increase the
repetition rate of dissolution DNP experiments will be
discussed. On the hardware side, the design of two multisample dissolution polarisers will be shown one of which
allows consecutive dissolutions with a minimum repetition
time of 3 minutes. Such fast repetition times are required for
cardiac imaging to follow the effects of coronary occlusion in
small animals. On the methodological side, we describe a
spin-thermodynamic model that allows the characterization of
nuclear polarizations during the DNP process or nuclear cross
polarization under thermal-mixing conditions. Such an
approach allows the prediction of polarization levels as a
function of the sample composition.
ThOB 11:35-11:50
Hybrid Polarizing Solids for Pure Hyperpolarized Liquids
through Dissolution Dynamic Nuclear Polarization
1
2
2
David Gajan ; Aurélien Bornet ; Basile Vuichoud ; Jonas
2
3
4
Milani ; Roberto Melzi ; Henri A. van Kalkerendd ; Laurent
4
4
5
Veyre ; Chloé Thieuleux ; Matthew P. Conley ; Wolfram R.
5
5
1
Gruning ; Martin Schwarzwalder ; Anne Lesage ; Christophe
5
2, 6
Copéret ; Geoffrey Bodenhausen ;
2
2
Lyndon Emsley ; Sami Jannin
1
2
ENS Lyon, Villeurbanne, France; EPFL, Lausanne,
3
4
Switzerland; Bruker Italia S.r.l, Milano, Italy; Université de
ABSTRACTS OF TALKS
5
Lyon, Lyon, France; ETHZ, Zurich, Switzerland;
6
ENS, Paris, France
We demonstrate that D-DNP can be performed efficiently with
a new generation of hybrid polarizing solids (HYPSO)
comprising TEMPO radicals incorporated in a mesostructured
silica material (Gajan D et.al. (2014) PNAS 111(41) :14693).
The powder is wetted with a solution containing metabolites or
other molecules of interest for MRS or MRI to fill the pore
channels (Incipient Wetness Impregnation), and DNP is
performed at low temperatures. During dissolution, the
HYPSO silica powder is retained by filtration close to the DNP
polarizer and a pure hyperpolarized solution can be
transferred to the NMR or MRI magnet within a few seconds.
The resulting solution of hyperpolarized metabolites is free
from any paramagnetic or toxic pollutants and ready for invivo infusion.
Jan Van Bentum; Manvendra Sharma; Gerrit Janssen; Jim
Leggett; Michael Tayler; Bas van Meerten; Arno Kentgens
IMM, Radboud University, Nijmegen, Netherlands
We present a novel approach to DNP enhanced NMR based
on rapid melting of a solid hyperpolarized sample followed by
'in-situ' NMR detection in the liquid state. The method
combines generic DNP enhancement in the solid state with
the high sensitivity of stripline 1H NMR detection in the liquid
state. Fast cycling facilitates options for signal averaging or
2D structural analysis. A second approach towards in-situ
high field liquid state DNP is based on the use of supercritical
solvents that allow for ultrashort Overhauser correlation times
between solute protons and radical electron spins.To study
the Overhauser mechanism for in-situ DNP, we explored the
temperature and radical-concentration dependence of the
relaxation in the supercritical phase of CO2/toluene mixtures.
ThOB 11:50-12:05
Efficient Dynamic Nuclear Polarization at 800 MHz with
Trityl-Nitroxide Biradicals
Guinevere Mathies
MIT, Francis Bitter Magnet Laboratory, Cambridge, MA
In recent years optimization of the chemical structure of
polarizing agents has, together with the development of
instrumentation, contributed tremendously to the increase of
the signal enhancement achievable by cross-effect DNP.
Hitherto the most successful polarizing agents were biradicals
consisting of two nitroxide moieties. We tested a new type of
biradicals, in which the narrow-line radical trityl is covalently
linked to a nitroxide, for cross-effect DNP at 211, 600, and
800 MHz. The best performing trityl-nitroxide biradical gives a
record enhancement of 65 at 800 MHz, with a polarization
build-up time of only 3.5 s. The experiments at multiple
frequencies show that for trityl-nitroxide biradicals the
enhancement through cross-effect DNP does not decrease
with the magnetic field.
10:45 AM – 12:30 PM, THURSDAY MORNING
Computational NMR: Predicting Spectra and
Chemical Shifts
Rafael Bruschweiler, presiding
Chapel
ThOB 12:05-12:20
Insights into DNP Mechanisms from Localized
Biradicals in the Dilute Limit
Rivkah Rogawski; Ivan Sergeyev; Yongjun Li;
Virginia Cornish; Ann McDermott
Columbia University, New York, NY
In overcoming the signal-to-noise barriers of solid state NMR,
cross-effect dynamic nuclear polarization (DNP) introduces
high concentrations of biradicals such as TOTAPOL.
Incorporating these compounds often presents solubility
challenges, and can introduce deleterious effects such as
paramagnetic bleaching/broadening. Additional insights into
the DNP mechanism and optimization of sample preparation
protocols are needed to extend the reach of this promising
technology. We utilize dihydrofolate reductase (DHFR) and its
TOTAPOL-derivatized
nanomolar
affinity
inhibitor
trimethoprim (TMP-T) to investigate DNP mechanisms. TMPT provides large enhancements down to 50 μM, approaching
concentrations required for in-vivo NMR, without degrading
spectral quality. Its high affinity for DHFR provides
unprecedented control over biradical localization, allowing
parameters such as the radius of paramagnetic bleaching at
100K to be measured.
ThOB 12:20-12:35
In-situ Rapid Melt DNP and Supercritical Overhauser
DNP, New Approaches towards Inline 1H NMR Detection
of Low Concentration Metabolites in Microfluidic Flow
ThOC 10:45-11:10
Estimating Chemical Shifts from Protein and
Nucleic Acid Structures
David Case
Rutgers University, Princeton, NJ
Chemical shifts provide important information about protein
and nucleic acid, structure but are often difficult to interpret in
any quantitative way. Quantum chemical studies using using
an automated fragment QM/MM scheme are now feasible
(within density functional theory), and we will present new
evidence of how accurate they may be expected to be for
globular proteins and nucleic acids. These ideas have been
incorporated into a new version of the SHIFTS program that
estimates shifts from structure for fairly general combinations
of proteins, nucleic acids and small-molecule ligands.
Questions remain (at this level) about how best to handle
solvent effects and geometry optimization, and different
possibilities will be discussed.
ThOC 11:10-11:35
Numerical Simulations of Solid-State NMR Experiments
1, 2
1
1
Zdeněk Tošner ; Niels Chr. Nielsen ; Thomas Vosegaard
1
Aarhus University, Aarhus, Denmark;
2
Charles University, Prague, Czech Republic
We will address several challenges associated with numerical
simulations of solid-state NMR experiments. We will give
examples on general-purpose simulations of dynamic
systems, combined molecular dynamics and NMR
simulations, new software for spectrum visualization, and
better ways of visualizing molecules and nuclear spin
interactions.
ThOC 11:35-12:00
SpinDrops: Visualizing the State and Dynamics of
Coupled Spin Systems
1
1
1
2
Ariane Garon ; Robert Zeier ; David Leiner ; Niklas J Glaser ;
1
1, 2
Michael Tesch ; Steffen Glaser
1
Technical Univ. Munich, Garching, Germany;
2
GlaserSystems, Garching, Germany
Visualization techniques are invaluable for understanding and
communicating abstract concepts and ideas, to think about
problems and to create innovative solutions. The novel
Page 41
ABSTRACTS OF TALKS
"DROPS" representation (discrete representation of operators
for spin systems) [1] nicely complements the classical vector
picture by mapping the non-classical states of coupled spins
to a set of characteristic "droplets". This makes it possible to
visualize abstract concepts, such as multiple-quantum
coherence and polarization transfer, in an intuitive way. The
DROPS representation has been implemented in the free
"SpinDrops" app [2], with which the rich dynamics of coupled
spins can be interactively explored.
1. Garon, R. Zeier, S. J. Glaser, arXiv:quant-ph/1409.5417.
2. N. J. Glaser, M. Tesch, S. J. Glaser, “SpinDrops”,
http://itunes.apple.com.
ThOC 12:00-12:15
Monitoring the Refinement of Crystal Structures with
Solid-State NMR Data – a Path to Ultra-High Resolution
Crystal Structures?
Jim Harper
University of Central Florida, Orlando, FL
Nearly a million crystal structures have now been deposited
into databases. It is known that many of these structures can
be improved by further refinement. The development of DFT
refinement methods that include lattice effects allows many of
these structures to be improved. Herein, NMR chemical shift
tensors are used to monitor DFT refinements of structures
from multiple sources. Both 13C and 15N tensors are shown
to be extremely sensitive to refinement and allow powder and
single crystal x-ray coordinates to be converted into structures
rivaling the most accurate data (i.e. single crystal neutron
diffraction). These comparisons suggest that even single
crystal neutron data can usually be improved to create ultrahigh resolution structures, surpassing the accuracy of the
original coordinates.
ThOC 12:15-12:30
A Revised NNLS Approach to
High-Resolution NMR Relaxometry
1
2
Robert J. Klingler ; Klaus Woelk
1
Argonne National Laboratory, Argonne, IL;
2
Missouri S&T, Rolla, MO
NMR relaxometry is a methodology to probe into the mobility
around NMR-active nuclei and determine porosity and pore
size distributions. When relaxation data are recorded from
samples with distributions of relaxation time constants,
calculations usually employ optimization procedures with
zeroth to fourth order regularizations. Because regularizations
prevent the detection of sharp features, a revised approach
without regularization is introduced reproducing delta
functions as well as distributions. T1 data of methane in the
pores of different clay materials were recorded using toroid
cavity probes. Because the revised approach is most
successful when data are collected as decaying toward zero,
inversion-recovery pulse experiments with phase-cycled split
inversion pulses are utilized, which simultaneously suppress
probe ring-down of the toroid cavity probe.
4:00 – 6:00 PM, THURSDAY AFTERNOON
Biosolids II
Chad Rienstra, presiding
Merrill Hall
ThOD 4:00-4:25
Advances in MAS Solid-State NMR using Deuterated
Microcrystalline Protein Samples
Bernd Reif
TU Munchen, Garching, Germany
Perdeuteration and back-substitution of exchangeable protons
in
microcrystalline
proteins
in
combination
with
recrystallization from D2O containing buffers reduces 1H, 1H
dipolar interactions such that amide proton line widths on the
order of 20 Hz are obtained. We show that a proton and a
carbon dilute sample is suited to access backbone 13Cα T1
relaxation times under fast MAS. We demonstrate that
TROSY type experiments are beneficial for the structural
characterization of residues in a protein which undergo ns-μs
dynamics. Furthermore, spin-state selective experiments can
be employed to yield high-resolution spectra under off-magic
angle conditions. Perspectives for the measurement of
distance restraints as well as for the quantification of order
parameters are discussed.
ThOD 4:25-4:50
Delving into the Unknown: Understanding How the
Molecular Structure of Tissues Drives Cell Behaviour
1
2
1
Melinda Duer ; Wing Ying Chow ; Rakesh Rajan ; Veronica
1
1
1
1
Wong ; David G Reid ; Dominique Bihan ; Richard Farndale ;
1
1
1
Chris Forman ; David Wales ; Roger Brooks
1
2
University of Cambridge, Cambridge, N/A; Leibnitz Institute
for Molecular Pharmacology, Berlin, Germany
The extracellular matrix provides the scaffold which supports
the cells of a tissue and essential cell signalling pathways.
However, understanding the molecular level properties of the
extracellular matrix has been hampered by the lack of
methods to study tissues at the atomic scale and chemically,
at a nanoscopic scale.
Here we show that using
13
13
multidimensional solid-state correlation NMR spectra ( C- C,
13
15
C- N) to fingerprint the underlying molecular structures in
native tissues from “heavy” mice allows us to understand key
molecular features and structural differences between tissues.
We have coupled this with NMR methods to examine the
chemical functionalities of collagen fibril surfaces, i.e. that
cells necessarily interact with, and how these change with
tissue damage, leading to altered cell behaviour.
ThOD 4:50-5:15
Perspectives for Proton-Detected Solid-State NMR
Sheng Qi Xiang; Suresh Kumar Vasa; Petra Rovó; Karin
Giller; Stefan Becker; Rasmus J. Linser
Max Planck Institute for Biophysical Chemistry,
Göttingen, Germany
Solid-state NMR has seen a large increase in possibilities
lately. Especially proton detection has provided manifold new
perspectives, ranging from facilitated backbone and sidechain
assignment to tools for characterization of structure and
dynamics. Importantly, the protein amount required for NMR
studies can be drastically reduced for proton-detected
methods employing a combination of fast spinning and high
degrees of protonation.
Employing fast and very fast Magic-Angle Spinning, we have
developed methods for resonance assignment and structure
Page 42
ABSTRACTS OF TALKS
elucidation of partially back-exchanged and fully protonated
proteins. These methods are based on the omission of scalarcoupling-based pulse sequence elements and the
employment of second-order Cross Polarization. We apply
these techniques to different proteins of general scientific
interest and conclude perspectives for complete abandonment
of deuteration.
ThOD 5:15-5:30
Line-Broadening in Low Temperature
Solid-State NMR Spectra of Fibrils
1
1
1
1
Thomas Bauer ; Claudio Dotta ; Livia Balacescu ; Julia Gath ;
1
1
2
Andreas Hunkeler ; Matthias Ernst ; Anja Böckmann ;
1
Beat Meier
1
2
ETH Zurich, Zurich, Switzerland; IBCP-CNRS, Lyon, France
In this work, we examine the residue-specific differences in
the temperature dependent line-broadening behavior of
uniformly labeled fibrillar HET-s (218 -289). We demonstrate
that, in contrast to the solvent-exposed parts of the protein,
the hydrophobic core residues show comparatively little
broadening in the temperature region between 273 K and 220
K. The line-broadening of the solvent exposed protein parts
appears to be strongly correlated to the successive decrease
in mobile water, which covers the protein surface even long
after the freezing of the excess bulk water. Further cooling
also changes the line width of the non solvent-exposed
protein parts, supporting the idea that an overall “freezing” of
motion in the protein affects the spectrum at very low
temperatures.
ThOD 5:30-5:45
15
Catalytic Roles of βLys87 in Tryptophan Synthase: N
Solid State NMR Studies
Bethany G. Caulkins; Chen Yang; Michael F. Dunn;
Leonard J. Mueller
University of California Riverside, Riverside, CA
The proposed mechanism for tryptophan synthase (TS)
shows bLys87 playing multiple catalytic roles: it bonds to the
PLP cofactor, activates C4' for nucleophilic attack via a
protonated Schiff base nitrogen, and abstracts and returns
15
protons to PLP-bound substrates.
ε- N-lysine TS was
15
prepared to access the protonation state of βLys87 using N
solid-state nuclear magnetic resonance for three stable
intermediates along the reaction pathway. These experiments
establish that the protonation state of the ε-amino group
switches between protonated and neutral states as the b-site
undergoes conversion from one intermediate to the next
during catalysis, corresponding to mechanistic steps where
this lysine residue has been anticipated to play alternating
acid and base catalytic roles that help steer reaction
specificity in TS catalysis.
ThOD 5:45-6:00
Reclaiming Resolution in DNP-SSNMR: Assignments and
Distances from Higher-Dimensional Experiments
1
2
3
4
Ivan Sergeyev ; Boris Itin ; Rivkah Rogawski ; Guohua Lv ;
4
3
David Eliezer ; Ann Mcdermott
1
Columbia University / New York Structural Biology, New
2
York, New York; New York Structural Biology Center, New
3
York, NY; Columbia University, New York, New York;
4
Weill Cornell Medical College, New York, NY
Dynamic nuclear polarization SSNMR spectroscopy has
dramatically reduced acquisition times and all but eliminated
the problem of being "signal limited." However, this does
come at a cost: DNP spectra typically have poorer resolution,
in many cases making 1D and 2D spectra largely unassignable. Here, we show that resolution can be improved in
biological DNP samples without sacrificing enhancement, and
that even modest gains in resolution yield assignable spectra
in higher-dimensional NCaCx/NCoCa-type experiments.
Further, we demonstrate that 3- and 4-dimensional sidechainsidechain sequential correlation experiments, designed to
"jump over" highly congested spectral regions such as the
carbonyl, greatly simplify assignments. We have successfully
applied these techniques to the study of various biological
samples, including amyloid fibrils and membrane proteins.
4:00 – 6:00 PM, THURSDAY AFTERNOON
Instrumentation
Jeff Reimer, presiding
Chapel
ThOE 4:00-4:25
Using Magnetic Coupling in High Resolution
NMR Circuits
Toby Zens; Paul Bowyer; James Finnigan; Brian Marsden;
Victor Lim; Bob Taber
Agilent Technologies, Santa Clara, CA
Magnetic coupling in NMR probe circuits is only sparingly
used today. However, in analyzing NMR probe circuits with
and without magnetic coupling it can be seen that not only can
you increase the experimental (function) capability of NMR
probes but also the performance and robustness of NMR
probes by using magnetic coupling. In this talk examples will
be shown on how to magnetic coupling can be used to
increase experimental capability. A novel new concept, the
circuit fill factor (CFF), will also be introduced. The CFF is a
handy and practical way of analyzing circuits for efficiency and
robustness. In using the CFF concept it can be shown that
magnetic coupling has a significant impact on NMR probe
circuits.
ThOE 4:25-4:50
Probing the Influence of Nuclear Spins on the MagnetoOptoelectronic Properties of pi-Conjugated Polymers
Christoph Boehme
University of Utah, Salt Lake City, UT
This presentation focuses on mechanisms that allow proton
spin states to influence magneto-optoelectronic properties of
organic semiconductors. Remarkably, even at low-magnetic
field conditions and room temperature, nuclear spin states
with energy splittings orders of magnitude below thermal
energies are able to influence observables like
magnetoresistance and fluorescence. While protons spins
couple to charge carrier spins via hyperfine interaction, there
has been considerable debate about the nature of the
electronic processes that are highly susceptible to these weak
hyperfine fields. Here, experiments are presented which show
how the manipulation of electron and nuclear spin states in a
pi-conjugated polymer device causes changes on the devices
currents. Implications of these experiments for the
understanding of the underlying electronic mechanisms are
discussed.
Page 43
ABSTRACTS OF TALKS
ThOE 4:50 - 5:15
Closed-Cycle Helium-Cooling MAS NMR Probe System
for Dynamic Nuclear Polarization at 16.4 T
1
2
2
Yoh Matsuki ; Toshitaka Idehara ; Yoshinori Tatematsu ;
3
4
1
Jagadishwar Sirigiri ; Shinji Nakamura ; Toshimichi Fujiwara
1
2
Osaka University, Suita, Japan; University of Fukui, Fukui,
3
4
JP; Bridge12 Technologies Inc., Framingham, MA; JEOL
RESONANCE Inc., Akishima, JP
Instrumentation for dynamic nuclear polarization (DNP)enhanced MAS NMR at very high field condition (B0 = 16.4 T)
is presented. The high field condition is crucial for gaining
spectral resolution and basic NMR sensitivity, but decreases
the DNP efficiency. To compensate for the loss, we have
developed a helium-spinning and -cooling MAS DNP NMR
probe system, where cryogenic helium gas is circulated in a
closed loop. This enabled us to sustain stable MAS (5kHz) at
cryogenic temperatures (>40K) for an extended period of time
(»6days) without consuming the cryogen gas. The low running
cost and easy operation of the system significantly broadens
the scope of the cryogenic MAS NMR and the high-field DNP
measurements to a wider range of users.
ThOE 5:15-5:30
Pre-clinical Magic Angle Field Spinning MRI Magnet for
Localized NMR Spectroscopy
Javier Alonso Valdesueiro; Cedric Hugon; Anne Soleilhavoup;
Angelo Guiga; Guy Aubert; Dimitrios Sakellariou
CEA Saclay, Gif-Sur-Yvette, France
Magic Angle Sample spinning is one of the cornerstones of
solid-state NMR. Most of anisotropic interactions can be
eliminated upon rapid sample rotation, leading to narrow highresolution NMR spectra. There are however many situations
where the sample cannot, or should not be spun rapidly, for
example in living tissues, in porous media, in heterogeneous
reactors and in energy materials. In these cases the
equivalent option of Magic Angle Field Spinning seems very
appealing.
Here we present the first preclinical 1.0T permanent magnet
for magic angle field spinning imaging and high-resolution
spectroscopy experiments.
ThOE 5:30-5:45
1.02 GHz LTS/HTS NMR: I. Development to Overcome the
Limitation of Magnetic Field Strength
1
2
2
Masato Takahashi ; Gen Nishijima ; Shinji Matsumoto ;
2
1
1
Kenjiro Hashi ; Seiya Iguchi ; Yoshinori Yanagisawa ; Hideaki
1
3
3
4
Maeda ; Takashi Miki ; Kazuyoshi Saito ; Ryoji Tanaka ;
4
4
4
Takahiro Nemoto ; Tetsuo Miyamoto ; Hiroto Suematsu ;
2
2
2
Takashi Noguchi ; Shinobu Ohki ; Atsushi Goto ;
2
Tadashi Shimizu
1
2
RIKEN CLST, Yokohama, Japan; National Institute for
3
Materials Science, Tsukuba, Japan; Kobe Steel Ltd., Kobe,
4
Japan; JEOL RESONANCE Inc., Akishima, Japan
Achieving a higher magnetic field is extremely important for
NMR
measurements.
However,
Low
Temperature
Superconducting (LTS) magnets are incapable to generate
the magnetic field exceeding 1 GHz (23.5 T). To exceed 1
GHz it is necessary to use high temperature superconducting
(HTS) magnets. Thus, we started a project to replace the
innermost Nb3Sn LTS coil of the 920 MHz NMR in NIMS
(Japan) by a Bi-2223 HTS coil. The LTS/HTS magnet was
completed and successfully achieved the world’s highest
NMR magnetic field, 1.02 GHz, in 2014. It was demonstrated
that the NMR spectrometer is basically usable for both
Page 44
solution NMR and solid-state NMR. This success will open up
a new world of super-high field NMR beyond 1 GHz.
ThOE 5:45-6:00
First NMR Results from an H/X/Y/e- CryoMAS-DNP Probe
Compatible with Closed-loop Spinning at 30 K
1
1
1
John Staab ; JB Spitzmesser ; Daniel Arcos ; George
1
1
1
1
Entzminger ; Judy Doty ; Vince Cothran ; Marc Bremmer ;
1
1
2
1
Glenn Doty ; David McCree ; Hiroto Suematsu ; Laura Holte ;
1
1
Paul Ellis ; F. David Doty
1
2
Doty Scientific, Inc., Columbia, SC; JEOL Resonance Inc.,
Tokyo, Japan
The H/X/Y/e- CryoMAS-DNP probe reported here, tested at
both 11.7 T and at 16.4 T, offers efficient microwave
irradiation for Dynamic Nuclear Polarization (DNP), full-range
H/X and H/X/Y tuning, sample VT from 30 - 380 K, closedloop spinning with cold helium gas, top sample loading, and
sample temperature independent of the rf coil temperature.
The biggest contribution to increased S/N comes
from being able to operate routinely down to 30 K –without
consuming helium. The second biggest improvement is in rf
noise temperature, TR. Additional improvements include
increased circuit efficiency and increased Q.
The presentation will discuss eight of the primary
challenges. Optimization methods included full-wave detailed
modeling of both the microwave (MW) system and the rf coil
system.
8:30 – 10:15 AM, FRIDAY MORNING
Dynamics: Methods and Applications
Teresa Carlomagno, presiding
Merrill Hall
FOA 8:30-8:55
Binding Pathways of Transient Protein Complexes
Studied by NMR Relaxation Dispersion Experiments
Anthony K Mittermaier
Mcgill University, Montreal, Canada
Little is known about the binding pathways of transient protein
complexes, since these are challenging to characterize
experimentally. We have shown that the combination of NMR
CPMG experiments and ITC can provide detailed information
on these systems. Applying these methods to a relatively
weak, short-lived SH3/peptide complex, we found that the
binding transition state is stabilized by long-range electrostatic
interactions while specific short-range contacts are absent. In
contrast, pressure-dependent NMR dynamics studies
indicated
that
both
solvent
and
conformational
rearrangements are nearly complete in the transition state.
Taken together, these results suggest that it is the disruption
of specific short-range contacts through small-amplitude
conformational rearrangements that triggers ligand release.
FOA 8:55-9:20
Dynamic Signatures of Active and Inhibited Protein
Kinase A using NMR Spectroscopy
Gianluigi Veglia
University of Minnesota, Minneapolis, MN
Protein kinases mediate a myriad of cell signaling events and
represent a major target for the pharmaceutical industry.
Protein kinase A (PKA) is a prototypical eukaryotic kinase,
sharing its catalytic core (PKA-C) with the Ser/Thr kinase
family. As PKA phosphorylates several substrates in different
tissues and is involved in pathologies such as
cardiomyopathies and cancer, it is important to understand
ABSTRACTS OF TALKS
the molecular mechanisms of substrate recognition and
specificity. X-ray crystallography has trapped PKA-C in
different conformational states along the enzymatic cycle.
However, these static structures do not fully explain the
mechanism for substrate recognition and, more importantly,
do not provide a signature for active and inhibited states. We
propose that structure and conformational dynamics (protein
flexibility) are equally important for defining active and
inhibited states as well as substrate recognition and product
release. To demonstrate this principle, we used solution NMR
spectroscopy to analyze PKA-C’s conformational dynamics
both in the slow and fast scale regimes. We found that the
slow time scale dynamics are linked with enzyme turnover.
Motions synchronous with kcat are initiated upon nucleotide
binding and pervade the entire enzyme, defining a
dynamically committed state. The inhibitor binding quenches
the enzyme’s conformational dynamics, creating a
dynamically quenched state. We also found an allosteric
mutant of PKA-C that shifts the timescale of the slower
dynamics. However, this altered flexibility reduces the
catalytic efficiency of the kinase. Unlike the backbone amide
groups, the conformational dynamics of the methyl groups in
the inner core of the kinase follow a different behavior, with a
decrease of flexibility both in the nucleotide and inhibitor
bound states, suggesting that backbone and side chains
reported on different phenomena.
In summary, the results presented establish that the dynamics
of ammonium ions within medium-sized proteins can be
quantified, thereby paving the way for the use of ammonium
spin-relaxation rates to characterize potassium-binding sites
in proteins.
FOA 9:20-9:45
Observing Short-Lived States in Proteins by Solid-State
NMR: New Methods Provide Insight into Functional
Dynamics of a Half-Megadalton Enzymatic Complex
Paul Schanda
Institut de Biologie Structurale, Grenoble, France
Protein function often relies on excursions to low-populated
transient states. Understanding such exchange processes is
therefore critical for understanding function. We present
recently developed methodologies that allow studying
conformational dynamics on micro/millisecond time scales by
solid-state NMR. We show that it is possible to obtain
information about thermodynamics and kinetics of such
exchange processes, as well as the structural propensities of
the involved transient states. After validating the approaches
on a well-characterized crystalline protein, it is demonstrated
that these solid-state NMR methods can provide insight into
hitherto hardly accessible very large proteins. We exemplify
this with the study of a half-megadalton large enzymatic
complex by provide evidence for functionally important
motions in entry pores of this complex.
8:30 – 10:15 AM, FRIDAY MORNING
The Quest for a Better Signal: Improving Sensitivity
and Resolution
Jeffrey Hoch, presiding
Merrill Hall
FOA 9:45-10:00
Characterizing Potassium Binding-Sites in Proteins by
15NH4+ NMR Spectroscopy
Nicolas Werbeck; D. Flemming Hansen
ISMB, Univ. College London, London, United Kingdom
Monovalent cations are known to regulate the function of
many enzymes. In previous studies from our laboratory we
used 15N-ammonium as a proxy for potassium to probe
potassium-binding sites in proteins by NMR spectroscopy.
Here we show pulse sequences to obtain the relaxation rates
of several spin-density elements of ammonium that, in turn,
are used to further characterize potassium binding-sites. For
example, an application to the DnaK protein (~40 kDa) shows
that the correlation time of an ammonium ion within a
potassium binding-site is 50ps.
FOA 10:00-10:15
Simultaneous Characterization of Spin Dynamics at Both
Fast (ps-ns) and Slow (μs-ms) Time Scales using
Adiabatic Spin-lock Experiments
Fa-An Chao; R. Andrew Byrd
National Cancer Institute, Frederick, MD
One of the most compelling advantages of NMR spectroscopy
is its ability to probe the conformational dynamics of
macromolecules at atomic resolution. A new approach is
proposed that uses data from adiabatic spin-lock experiments,
which allows us to simultaneously extract dynamic parameters
at both fast (ps-ns) and slow (μs-ms) time scales. Based on
simulations and experimental tests on two different biological
samples, the new approach can provide accurate dynamic
parameters when the data sets from two magnetic fields are
available. We found that this new approach not only
simultaneously characterizes the conformational dynamics at
two different time scales, but also expands the range of slow
conformational dynamics which can be probed by current
relaxation experiments.
FOB 10:45-11:10
Enhancing the Resolution of Proton-detected NMR
Spectra by Spatially-selective Excitation
Klaus Zangger; N.Helge Meyer; Simon Glanzer; Nina
Gubensäk; Johannes Mauhart
University of Graz, Graz, Austria
Homonuclear broadband decoupling, vastly increases the
resolution of proton spectra. One of the approaches for
broadband homodecoupling in the indirect dimension of
multidimensional NMR spectra uses frequency-selective
pulses during a weak gradient field. We recently reported an
adaption of this method to achieve broadband
homodecoupling during acquisition. This is achieved by
interrupting the acquisition of the FID after each data chunk
and refocusing of scalar coupling by slice-selective inversion.
Coupling information, which is often key in analyzing chemical
structures, is of course completely lost in such experiments.
To obtain J values with high resolution, it is possible to record
NMR spectra which contain scalar coupling to one selected
signal only or to reduce coupling constants by any desired
value.
FOB 11:10-11:35
Parahydrogen Induced Polarization by Pairwise
Replacement Catalysis
1
1, 2
1
Clifford R Bowers ; Ronghui Zhou ; Evan Zhao ; Wei
3
3, 4
3
Cheng ; Luke Neal ; Haibin Zheng ;
3
Helena Hagelin-Weaver
1
Chemistry, University of Florida, Gainesville, Florida;
2
Colgate-Palmolive Technology Center, Piscataway, New
3
Jersey; Chemical Engineering, University of Florida,
4
Gainesville, FL; NC State University, Raleigh, NC
Page 45
ABSTRACTS OF TALKS
Supported metals are used extensively in industrial
hydrogenation and offer important advantages over
homogeneous catalysis, including ease of separation of the
product and compatibility with a continuous-flow reactor
configuration. In view of the sequential step-wise nature of Hatom addition in the standard mechanism of hydrogenation
over supported metals like Pt, the observation of intense PHIP
NMR signals using such catalysts came as a welcome yet
unexpected development. Perhaps even more remarkably,
supported Pt and Ir nanoparticles are shown herein to
catalyze
pairwise
replacement
on
propene
and
trifluoropropene. By simply flowing a mixture of p-H2 and
substrate over the catalyst, the symmetrization order is
incorporated into the substrate without a change in molecular
structure, producing intense PHIP NMR signals.
FOB 11:35-12:00
Theorems for the Sensitivity Advantages of
Nonuniform Sampling
1
1
3
David Rovnyak ; Melissa Palmer ; Christopher Suiter ;
5
4
2
Geneive E. Henry ; James Rovnyak ; Jeffrey C. Hoch ;
3
Tatyana Polenova
1
2
Bucknell University, Lewisburg, PA; Univ of Connecticut
3
Health Ctr, Farmington; University of Delaware, Newark;
4
University of Virginia, Charlottesville, VA;
5
Susquehanna University, Selinsgrove, PA
Many multi-dimensional experiments in nuclear magnetic
resonance spectroscopy can benefit from a signal-to-noise
ratio (SNR) enhancement up to about two-fold if a decaying
signal in an indirect dimension is sampled with
nonconsecutive increments, termed non-uniform sampling
(NUS). This work provides formal theoretical results and
applications to resolve major questions on the scope of the
NUS enhancement for recording exponentially decaying
signals. Formally proved, two theorems will be presented
describing separate aspects of the sensitivity advantages of
NUS over uniform sampling. Example applications of these
principles are given for protein, biosolids, and natural products
NMR.
Page 46
FOB 12:00-12:15
Slice-Selective NMR : Toward Fully Resolved Correlation
Spectroscopy
Nicolas Giraud
Universite Paris-Sud, Orsay, France
The quest for higher resolution in nuclear magnetic resonance
has been enlightened over the last years by the
breakthroughs accomplished in the field of slice-selective
NMR. We will present our latest theoretical and experimental
developments in this field, that allow for designing correlation
spectra in a fully tailored manner. Two novel correlation
experiments will be discussed. On the one hand, the PCRCOSY allows for combining pure shift and J-edited spin
evolutions by coding them along different gradient axes, in
order to acquire a general correlation spectrum. On the other
hand, the push-G-SERF experiment allows for fully resolving
both dimensions of the spectrum, yielding a straightforward
assignment and measurement of the coupling network around
a selected proton in the molecule.
FOB 12:15-12:30
Quantitative Trace Analysis of Complex Mixtures Using
SABRE Hyperpolarization
Nan Eshuis; Bram J. A. van Weerdenburg; Martin C. Feiters;
Floris P.J.T. Rutjes; Sybren S. Wijmenga; Marco Tessari
Radboud University, Nijmegen, Netherlands
We investigate possible applications of nuclear spin
hyperpolarization in the trace analysis of complex mixtures. In
order to obtain nuclear spin hyperpolarization, we use parahydrogen (p-H2) in a method called SABRE, which is based
on the reversible interaction of p-H2 and substrate molecules
[1]
at a metallo-organic complex.
A transient scalar coupling
network within this complex allows the transfer of spin order
from p-H2 to the nuclear spins of the substrate, resulting in
strongly enhanced NMR signals. The present study shows
that it is feasible to combine such an increase in sensitivity
with a quantitative analysis of complex mixtures, implicating
[1]
potential applications of SABRE in analytical chemistry.
Adams R. W. et al. Science (2009), 323, 1708-1711.
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
Biomolecules in Solution.............................................. 001-070
Biomolecules in the Solid-State ................................... 071-117
Dynamics ..................................................................... 118-142
Computational NMR .................................................... 143-169
MRI/MRS ..................................................................... 170-209
Exotica ......................................................................... 210-228
Hyperpolarization and DNP ......................................... 229-275
Small Molecules........................................................... 276-333
Drug Discovery ............................................................ 334-344
Metabolomics .............................................................. 345-366
Materials and Inorganics.............................................. 367-421
Instrumentation ............................................................ 422-469
Monday/Tuesday Short Talks ...................................... 470-484
Wednesday/Thursday short Talks ............................... 470-484
BIOMOLECULES IN SOLUTION
001 - 070
Poster 001
Structure and Function of Ribosomal Biogenesis Factor
Nsa2
1
1
2
1
Sarah Clark ; Afua Nyarko ; Ed Hurt ; Elisar Barbar
1
2
Oregon State University, Corvallis, Oregon; Biochemistry
Center of Heidelberg University, Heidelberg, Germany
Eukaryotic ribosome biogenesis is a complex process that
involves the participation of over 200 assembly factors.
Among these factors is Nsa2, a protein that aids in
establishing a physical link between the Rea1 ATPase and
helix 89 of the preribosome. Here we report the NMR solution
structures for the N-terminal and C-terminal domains of Nsa2.
Fitting of these structures into a cryo-EM model of the pre-60S
ribosome revealed a possible role for Nsa2 as a “clamp” that
helps move helix 89 to its final position on the mature
ribosome. Our findings suggest a functional role for Nsa2 in
the ribosome biogenesis network and illustrate the power of
NMR in combination with other structural techniques to gain
insight into biological processes.
Poster 002
The Ligand-TPPI NOESY: Obtaining Higher Quality
Structures of Protein-Ligand Complexes Using Just One
Experiment
1
1
2
Alvar Gossert ; Chrystèle Henry ; Elena Schmidt ; Julia M.
2
2
Weber ; Peter Güntert
1
Novartis Institutes of BioMedical Research, Basel,
2
Switzerland; Goethe University, Frankfurt am Main, Germany
The Ligand-TPPI NOESY is a combined 3D HSQC-NOESY
13
15
containing all signals of C/ N-edited NOESYs as well as
intra-ligand and inter-molecular NOEs.
Signals of the
unlabeled ligand are recorded in a homonuclear ‘ligand-plane’
in the 3D NOESY. Using an adapted TPPI scheme, ligand
signals are not suppressed but are artificially moved to 100
13
ppm in the C-dimension. Therefore, all NOEs needed for a
structure calculation are recorded in one spectrum, typically
over a weekend. We show that this approach yields structures
of superior quality than conventional approaches.
Further advantages of the Ligand-TPPI experiment are shown
with results from several types of ligands, covering peptides
with internal structure, organic compounds with strong
chemical shift changes and fragments with long T1 relaxation.
Poster 003
Solution Conformation of the Unbound HIV-1 Protease
Derived from Residual Dipolar Couplings Measured at
Ambient and High-Pressure Conditions
Julien Roche; John M. Louis; Ad Bax
NIH, Bethesda, MD
While hundred of crystal structures of protease-inhibitor
complexes have been solved, only a dozen of free protease
structures have been reported. We determined the flap
orientation of the unbound protease by comparing the
measured residual dipolar couplings to reference crystal
structures representing the closed, semi-open and wide-open
states. The data clearly indicate that the apo protease adopts
a closed conformation in solution, similar to an inhibitor-bound
state. We also compared the effect of high-pressure on the
flap conformations by measuring residual dipolar couplings at
600 bar. While a minimal rearrangement of the flaps was
observed in the case of the inhibitor-protease complex, we
observed a significant pressure-induced rotation of the flaps in
the case of the unbound protease.
Poster 004
NMR Characterization of the Interaction of the
Endonuclease Domain of MutL with Divalent Metal Ions
and ATP
Ryota Mizushima
RIKEN Quantitative Biology Center (QBiC), Suita, Japan
DNA mismatch repair (MMR) is the process of rectifying postreplicative base pair errors, thereby enhancing the fidelity of
DNA replication 100-1000 fold. MutL plays a central role in
MMR. MutL is a multi-domain protein comprising an Nterminal ATPase domain (NTD) and C-terminal dimerization
domain (CTD), connected with flexible linker regions. To
understand the regulation mechanism underlying MutL
endonuclease activity, our NMR-based study investigated
interactions between the bacterial MutL-CTD and binding
molecules. Peak intensity analysis indicated the binding site
2+
for Mn . Chemical shift perturbation revealed a novel ATP
binding site in MutL-CTD. A docking simulation provided a
putative scheme for the intermolecular interactions between
MutL-CTD and ATP. We proposed a mechanical model for the
regulation of MutL endonuclease activity in MMR.
Poster 005
Characterization of the Hydroxyproline-induced Kink in
the Solution Structure of Conantokins
Yue Yuan; Shailaja Kunda; Jaroslav Zajicek;
Francis J. Castellino
University of Notre Dame, Notre Dame, IN
Conantokins are naturally occurring, γ-carboxyglutamate (Gla;
γ)-containing neuroactive peptides, which are synthesized by
marine snails, and known to be N-methyl-D-aspartate (NMDA)
receptor antagonists. A recently discovered conantokin Rl-B
(ConRl-B) uniquely differs from other conantokins by the
presence of a 4-hydroxyproline (Hyp, ‘O’) residue, which kinks
the α-helices that exist in conantokins. Two mutant peptides,
Con-G[10▼O] and ConRl-B[∆KAO, ▼NQ], have also been
synthesized to correlate helix disruption with activity. We have
determined the solution structures of these three peptides
using 2D NMR; the structures provide new insight into
conantokin structure-function relationship.
Page 47
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
Poster 006
A Rapid and Efficient Method for Collection of eNOE for
Larger Proteins: An Application to Ensemble Structure
Calculation
1
1
2
3
Chi Celestine ; Dean Strotz ; Roland Riek ; Beat Vogeli
1
2
ETH, Zurich, Zurich, Switzerland; ETH Zurich, Zurich,
3
Switzerland; Swiss Federal Institute of Technology, ETH
Zurich, Zürich, Switzerland
The representation of a protein’s spatial sampling at atomic
resolution is fundamental for understanding its function. NMR
has been established as the best-suited technique toward this
goal for small proteins. However, the accessible information
content rapidly deteriorates with increasing protein size. We
have recently demonstrated that for small proteins distance
restraints with an accuracy smaller than 0.1 Å can be obtained
by replacing traditional semi-quantitative Nuclear Overhauser
Effects (NOEs) with exact NOEs (eNOE). The high quality of
the data allowed us to calculate structural ensembles of the
small model protein GB3 consisting of multiple rather than a
single state. The eNOE analysis has been limited to small
proteins because cross peaks arising from spin pairs with
overlapped diagonal peaks cannot be converted into exact
distance restraints. Here we propose a simplified approach to
translate NOEs into correct upper distance restraints, which
opens access to larger biomolecules. We demonstrate that for
the 16 kDa cis/trans isomerase human cyclophilin A the
collection of such restraints extends the original 1254 eNOEs
to 3471.
Poster 007
F-NMR Paramagnetic Relaxation Enhancement in
Proteins
Elena Matei; Angela M. Gronenborn
University of Pittsburgh, Pittsburgh, PA
Fluorine NMR Paramagnetic Relaxation Enhancement for the
extraction of distance information in selectively F-labeled
proteins was explored using the HIV-inactivating lectin
Cyanovirin-N.
19
F was introduced at the 4-, 5-, 6- and 7 position of the single
Tryptophan and positions 50 and 52 in the protein sequence
were selected for attachment of the paramagnetic MTSL label.
Q50C and S52C variants were created by mutagenesis and
MTSL-tagged (paramagnetic and diamagnetic) modified
15
uniformly N labeled proteins with singly F labeled Trp49
19
were used.A series of 1D F –T2 NMR spectra were recorded
at 298 K using different relaxation delays. For each sample,
19
the extracted transverse F- PRE rate, Γ2, was used to
19
determine the average distance between the F nucleus and
the paramagnetic center.
Poster 008
Solution Structure of HMG Box 456 of Human Upstream
Binding Factor (hUBF) with Segmental Isotopic Labeling
Technique
1, 2
2
2
2
Fangling Ji ; Jiahai Zhang ; Ke Ruan ; Jihui Wu ;
2
Yunyu Shi
1
2
DLUT, Dalian, China; USTC, Hefei, China
HMG box 456 from human upstream binding factor (hUBF)
were segmental isotopic labeled by protein trans-splicing
(PTS) in vivo. We have determined the solution structure and
characterized the dynamic behavior for selectively segmental
labeled protein regions on the recombinant expressed hUBF
protein by NMR, respectively. The overall solution structure of
Page 48
HMG box 456 were refined by distance restraints generated
13
from inter-domain three-dimensional (3D) simultaneous C
15
and N NOESY experiments and residual dipolar couplings
(RDCs).
Poster 009
Isotope Effects on Fast NH and ND Exchange Rates in
Tryptophan by NMR
1, 2
1, 2
2
Estel Canet ; Pavel Kaderavek ; Philippe Pelupessy ;
1, 2
Geoffrey Bodenhausen
1
2
EPFL, Lausanne, Switzerland; ENS, Paris, France
The determination of exchange rates of labile hydrogens in
proteins is important for understanding their function, as it
provides a rich source of structural and dynamic information.
The measurement of H/H and D/D exchange rates of the NH
or ND groups of the indole ring in tryptophan and the
comparison of them describes an isotope effect, which is one
of the most sensitive tools for the study of reaction
mechanisms, as it can give insight into thermodynamic
parameters that describe the stability of hydrogen-bonded
secondary structures under different environments. The
-1
exchange rate for protons is kH = 213 s and for deuterium is
-1
kD = 110 s at pH 8.3 and 300 K. The isotope effect is kH/kD ≈
2.
Poster 010
Real-time NMR Spectroscopy of Human γD Crystallin
Unfolding with Metal Ions
Lina Rivillas-Acevedo; Carlos Amero
LABRMN-CIQ, UAEM, Cuernavaca, Mexico
Cataract is one of the mayor cause of blindness worldwide,
and it is characterized by protein aggregation inside the eye,
causing lens opacity. Age, UV radiation and metals are some
of the causes of protein damage that may induce this
aggregation. It has been found that micromolar concentrations
of copper ions induce the aggregation of human γD crystallin
(HγD). HγD is a highly stable protein with 173 aminoacids
forming two homologous domains, each containing two Greek
key motifs. In order to get a better understanding of the
cataract formation process, we have identified the specific
metal binding sites and we have characterized the unfolding
of HγD in the presence of Cu(II) with atomic resolution using
Real-time NMR spectroscopy.
Poster 011
Binding of Glycosaminoglycans to Interleukin-10 by NMR
Spectroscopy
1
2
2
Georg Künze ; Jan-Philip Gehrcke ; Mayte Pisabarro ;
3
3
1
Sebastian Köhling ; Jörg Rademann ; Daniel Huster
1
2
University of Leipzig, Leipzig, Germany; BIOTEC TU
3
Dresden, Dresden, Germany; Free University Berlin,
Berlin, Germany
The cytokine interleukin (IL)-10 is a key protein of the immune
system, which prevents an overwhelming immune reaction
and tissue damage. It was shown to be regulated by
glycosaminoglycans (GAGs) – a class of highly sulfated
carbohydrates within the extracellular matrix that play a
decisive role in the biology of many cytokines e.g. for receptor
binding or protection from proteolytic degradation. The
structural characterization of protein-carbohydrate complexes
is often impeded by weak ligand affinity and the paucity of
non-exchangeable protons at close distances as requirement
for a NOE-based structure determination. Here, we used a
combination of ligand-detected NMR-methods (i.e. STD,
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
transferred NOESY) along with experiments based on proteinand ligand-immobilized paramagnetic spin labels to determine
the structure of the GAG-IL-10-complex.
Poster 012
NMR Studies of the Cytoplasmic Domains of Membrane
Anchored Transcription Factors from
Gram-Negative Bacteria
1
1
1
Sergio-Andres Pulido ; Evelyne Schrank ; Gabriel Wagner ;
2
1
Helge Meyer ; Klaus Zangger
1
2
Karl franzens University-Graz, Graz, Austria; Klinik Allg.
Visc. Chir. Klin. Oldenburg, Germany, Oldenburg, Germany
The transcriptional control of genes coding the protein toxins
in Gram-negative bacteria is performed either by cytoplasmic
soluble elements or transmembrane proteins with at least one
DNA-binding cytoplasmic domain. The cytoplasmic domains
of this kind of transcription factors is responsible for the
recognition of the DNA transcription elements and the
interactions with other transcription factors. Here we report the
solution NMR studies of the cytoplasmic domains of the
bitopic transcriptional regulators of ToxT. This is the first
atomic resolution evidence about this two-component system
at the cytoplasmic level. The presented structural data on the
cytoplasmic domains of membrane-associated transcription
factors in bacteria should help to better understand the
regulation of virulence factors in gram-negative pathogens.
Poster 013
Backbone Dynamics Study of Type III Antifreeze Proteins
Explains Their Different Antifreezing Activities
Yong-Geun Choi; Joon-Hwa Lee
Dept of Chemistry, Gyeongsang National University,
Jinju, South Korea
Antifreeze proteins (AFPs) are found in a variety of coldadapted organisms to promote survival at subzero
temperatures by binding to ice crystals and decreasing the
freezing temperature of body fluids. The type III AFPs have
been categorized into two subgroups, quaternary-amino-ethyl
(QAE) and sulfopropyl (SP) Sephadex-binding, based on
differences in their isoelectric points. The QAE proteins can
be further divided into two subgroups, QAE1 and QAE2.
Among them, only the QAE1 isoforms exhibit full thermal
hysteresis (TH) activities, whereas the others have extremely
low or no such activities. In this study, we have performed
backbone dynamics analyses of three kinds of type III AFPs
from Zoarces elongatus Kner, nfeAFP8 (QAE1), nfeAFP11
(QAE2), and nfeAFP6 (SP) at various temperatures.
Poster 014
Molecular Insights into Kinase-Cochaperone Recognition
Dimitra Keramisanou; Devon Marshall; Ziming Zhang;
Ioannis Gelis
University of South Florida, Chemistry, Tampa, FL
Cdc37 is a cochaperone that acts at an early stage of the
Hsp90 chaperone cycle by recruiting kinase substrates to
Hsp90. Despite being an essential component of the Hsp90
machinery, the molecular mechanism by which it recognizes
kinases and facilitates their interaction with Hsp90 is poorly
understood. We have used high-resolution NMR spectroscopy
to characterize the principles underlying kinase recognition
and sorting.
Poster 015
13
Direct C-detected Experiments for the Investigation of
Hydrogen Bond mediated Interactions in Nucleic Acids
1
1
1
Boris Fürtig ; Christian Richter ; Robbin Schnieders ; Helena
2
1
Kovacs ; Harald Schwalbe
1
2
Goethe University, Frankfurt, Germany; Bruker Biospin AG,
Fällanden, Switzerland
Hydrogen bond mediated interactions between nucleo-bases
represent one of the major secondary and tertiary structure
forming principles in RNA and DNA molecules.
Characterization of these interactions allows the delineation of
the structure, the stability and the dynamic behavior of certain
structural elements that are the building blocks of biological
RNA molecules.
13
Here we present new C-direct detected NMR experiments
that allow the characterization of hydrogen-bonding
interactions in nucleo-bases of RNA molecules. In these
experiments the imino-proton is not any longer used as a
13
15
C- N
reported signal but it is used to dephase
magnetization. The experiment can be used to determine the
solvent exchange rate and the 1JNH coupling constant.
Poster 016
NMR used for the Structural Characterization of
Therapeutic Antibodies
1
1
1
Alfred Ross ; Fabio Casagrande ; Martin Binder ;
2
Pierre Goldbach
1
Hoffmann LaRoche AG - Disovery Technologies, Basel,
2
Switzerland; Hoffmann LaRoch AG - Technical Development,
Basel, Switzerland
We show how homo- and heteronuclear multidimensional
NMR is used for the characterization of therapeutic antibodies
or related Fab fragments thereof. This includes applications
for the characterization of
•
Oxidation of methionines and tryptophanes
•
Cystinylation of the antibody with cysteine used as
formulation excipient
•
Characterization of diffusion behavior
In addition we propose a low-viscosity organic solvent which
allows acquisition of good-quality NMR data even for
unstructured high molecular weight proteins.
Poster 017
Structure of the Mitochondrial Translocator Protein in
Complex with a Diagnostic Ligand.
1, 2
2
2
Lukasz Jaremko ; Mariusz Jaremko ; Karin Giller ; Stefan
2
1, 2
Becker ; Markus Zweckstetter
1
Deutsches Zentrum für Neurodegenerative Erkrankung,
2
Goettingen, Germany; Max-Planck-Institut für
Biophysikalische Chemie, Goettingen, Germany
The 18-kilodalton translocator protein TSPO is found in
mitochondrial membranes and mediates the import of
cholesterol and porphyrins into mitochondria. In line with the
role of TSPO in mitochondrial function, TSPO ligands are
used for a variety of diagnostic and therapeutic applications in
animals and humans. We present the three-dimensional highresolution structure of mammalian TSPO reconstituted in
detergent micelles in complex with its high-affinity ligand
PK11195. The TSPO-PK11195 structure is described by a
tight bundle of five transmembrane a helices that form a
hydrophobic pocket accepting PK11195. Ligand-induced
stabilization of the structure of TSPO suggests a molecular
Page 49
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
mechanism for the stimulation of cholesterol transport into
mitochondria.
Poster 018
NMR Analysis of Natural Conus Peptides and Designed
Synthetic Foldamers Hybrids.
S. Raghothama
Indian Institute of Science, Bangalore, India
Proline in contraphans made-up of cyclic disulfide peptides
leads to formation of cis-trans isomerization. Two peptides,
Conus-Loroisii (Lo959:GCPDWDPWC) and conus virgo
(vi804:CIWPWC) along with a
analog DW3-Vi804
(CIDWPWC) is considered for study. NMR results in Lo959
existing in two distinct cis and trans form simultaneously.
Such “shape-shifting” molecules are of interest as they can
bind to multiple receptors. Vi804 exists only cis form but its
analog flips to trans. NOEs establish aromatic proline
interactions in the WPW motif.
In another project synthetic hybrids incorporating residues are
studied. Use of constrained / unconstrained residues into
sequences yielded varying expanded helices. Getting sheets
seems difficult in such sequences. Only in case of Boc[4(R)Val]n-OMe when n=4, a sheet was observed.
Poster 019
Probing Protein Quinary Structures by in-cell NMR
Subhabrata Majumder; Jing Xue; Christopher DeMott; Sergey
Reverdatto; David Burz; Alexander Shekhtman
University at Albany, Albany, New York
Historically introduced by McConkey to explain the slow
mutation rate of highly abundant proteins, protein quinary
structures are an emergent property of living cells. The
protein complexes that constitute quinary structures are
transient and thus difficult to study biochemically in vitro.
Cross-Relaxation Induced Polarization Transfer, CRIPT,
based in-cell NMR allows the characterization of protein
quinary structures with atomic resolution in-side live
prokaryotic and eukaryotic cells. We show that RNAs are an
important component of protein quinary structures. Protein
quinary structures are unique to the target protein and affect
physicochemi-cal properties, protein activity, and interactions
with drugs.
Poster 020
Structure of Domain 1.1 of Sigma A Factor of RNA
Polymerase from Bacillus subtilis
1, 2
1, 2
3
Milan Zachrdla ; Lukáš Žídek ; Alžběta Rabatinová ; Hana
3
3
Šanderová ; Libor Krásný
1
NCBR, Faculty of Science, Masaryk University, Brno, Czech
2
Republic; CEITEC, Masaryk University, Brno, Czech
3
Republic; Academy of Sciences of the Czech Republic,
Prague, Czech Republic
RNA polymerase of gram-positive bacteria contains several
unique subunits in comparison to RNA polymerase of gramnegative bacteria. Sigma subunits play a critical role in
recognition of DNA promotor sequence. In order to improve
our understanding of transcription mechanisms we solved the
structure of auto-regulating domain 1.1 of sigma A factor from
Bacillus subtilis. Sigma 1.1 is a 9.3 kDa N-terminal domain
connected to the rest of the sigma factor by a flexible linker.
Solution state NMR spectroscopy was used to obtain interatomic distances from experiments based on nuclear
Overhauser effect (NOE). The experiments were performed
Page 50
on a 13C, 15N fully-labelled protein using 850 MHz
spectrometers. The structural part of our study will be followed
by relaxation analysis of molecular motions.
Poster 021
Structural Characterization of the Interaction between
Ubiquitin Specific Protease 7 and Icp0 from HSV1 Virus
Alexandra Pozhidaeva; Dmitry Korzhnev; Irina Bezsonova
UCONN Health Center, Farmington, CT
USP7 is a deubiquitinating enzyme that regulates cellular
levels of multiple proteins. Its inhibition was shown to be
beneficial for treatment of myeloma and colon carcinoma,
which makes USP7 an attractive drug target. Currently all
USP7 inhibitors target its catalytic activity only. C-terminal
region of USP7 consists of five ubiquitin-like domains (UBL15) comprising several substrate-binding sites. Affecting
USP7/substrate binding interfaces might be a more targetspecific way of regulating USP7 activity. Here we present the
first structural characterization of USP7 substrate recognition
by its UBL domains. Using NMR spectroscopy we showed
that Icp0 protein from Herpes Simplex virus 1 interacts with
UBL1-2 domains and mapped the Icp0 binding site on the
surface of USP7.
Poster 022
Combining Small Angle Neutron Scattering and NMR Data
to Determine the Structure of the Box C/D Holo-Enzyme
1
1
1
Bernd Simon ; Audrone Lapinaite ; Andrea Graziadei ;
1
1
2
Alexander Marchanka ; Pawel Masiewicz ; Frank Gabel ;
1
Teresa Carlomagno
1
European Molecular Biology Laboratory, Heidelberg,
2
Germany; Institut de Biologie Structurale and Institut Laue,
Grenoble, France
The Box C/D enzyme is a 390 kDa RNA-protein complex that
methylates ribosomal RNA. It is composed of four copies of
three different proteins L7Ae, Nop5 and fibrillarin that
assemble on two copies of the guide RNA molecule, each of
which is the template for two different target RNAs. We
obtained structural models for the apo and holo form of the
enzyme by an integrated structural approach employing
paramagnetic relaxation enhancements (PRE), small angle
neutron scattering (SANS) with contrast variation and pulsed
EPR (PELDOR) experiments. The structures reveal a
sequential methylation of the physiological substrates and
different conformations depending on the occupancy of its
target binding sites.
Poster 023
Revealing the Structural and Thermodynamic Basis for
the Cooperative Binding and Selective Retention of
Proteins in Multimodal Chromatography
Kartik Srinivasan; Maria Lopez; Steven Cramer;
Scott McCallum
Rensselaer Polytechnic Institute, Troy, NY
For many proteins, multimodal (MM) chromatographic
resin systems create exclusive windows of selectivity as
compared to traditional single mode chromatographic
systems. Reported here are results from NMR- and ITCbased methods being developed that provide insight into how
multiple interaction modes utilize binding cooperativity among
multiple resin-protein contacts to create unique protein binding
selectivities. To accomplish these goals, mimics of resin
surfaces have been created using gold nanoparticles
functionalized with chromatographic resin groups where these
POSTERS
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
particles are amendable to NMR analysis and the density of
the functionalization can be controlled. The insights gained
from this fundamental work are being employed in concert
with
MD
simulations to create predictive models for
improving the separation capabilities of industrial process
mixtures.
the p62/Tfb1 subunit of TFIIH. The structure reveals that p65TAD forms an 11-residue α-helix when bound to Tfb1.
Comparison with other structures of TADs bound to Tfb1
reveals several interesting difference. The implications of
these differences will be discussed, as it is unique in TADs
and likely to affect the affinity with other transcription factors.
Poster 024
Structural Characterization of Melanoregulin (dsu): The
Protein Involved in Regulation of Cell Pigmentation
Ashok Rout; Marie-Paule S; John A Hammer; Nico Tjandra
National Institutes of Health, Bethesda, MD
Motor protein myosin (MYO5a) and its receptor
RAB27A/MLPH transfers melanosomes to the surrounding
keratinocytes, required for mammalian pigmentation. Mutation
in this motor-receptor complex makes the melanosomes
transfer uneven, resulting in coat color dilution. However,
mutation of a fourth gene; melanoregulin (dsu) is found to
suppress this coat color dilution, independent of the MYO5a
pathway. Our structural studies showed that dsu has α-helical
conformation. PREs obtained by attaching paramagnetic
reagent PROXYL to different positions in dsu revealed that
these helices are close to each other to form a compact
structure. Thus, 3D structure determination of dsu could
provide important structural information’s, which can further
be used for predicting the mechanism of this coat color
dilution and general biological function of dsu.
Poster 027
NMR Observation of the Binding of Odorants to the
Mouse Odorant Receptor MOR244-3
Jessica Burger; Kavita Jeerage; Thomas Bruno
NIST, Boulder, CO
Mammals are able to perceive and differentiate a large
number of structurally diverse odorants through the odorant’s
interaction with odorant receptors (ORs). The natural gas
industry has utilized human sensitivity to thiols to increase the
safety of fuel gas transport, storage, and use through
odorization. Due to the low affinity of odorous ligand for the
ORs and difficulty in expressing a sufficient amount of
receptor proteins, it has been challenging to directly measure
binding of odorants with ORs, and therefore difficult to
fundamentally understand odorization. In order to better
understand the mechanisms associated with the detection of
thiols, we have directly observed the binding of 2methylpropane-2-thiol to mouse MOR244-3 on living cells by
saturation transfer difference nuclear magnetic resonance
spectroscopy.
Poster 025
Characterization of the Sparsely Labeled Glycosylated
Protein, Robo1, by NMR
Qi Gao; Shuo Wang; Chengli Zong; Kelley Moremen; GeertJan Boons; James Prestegard
Complex Carbohydrate Research Center, Athens, GA
Many mammalian proteins require glycosylation for proper
function. Therefore, biophysical characterization, including
structure, is best done on properly glycosylated forms
produced by expression in mammalian cell culture. This
presents a challenge for NMR characterization using
conventional methodology, because of the expense of uniform
isotopic labeling and an inability to perdeuterate. We
demonstrate an alternative methodology using sparse labeling
with single 15N enriched amino acids, combined with the high
structural content experiments generating long range
paramagnetic and orientational constraints. A two domain
construct from Robo 1, a cell surface signaling molecule
important in axon guidance during development that binds
heparan sulfate, is used to illustrate the methodology. A
model showing the bound geometry for a heparan sufate
tetrasaccharide has been derived.
Poster 028
Solution-state NMR Investigation of Cold Adaptation in
Antarctic Toothfish Lens Proteins
Jan Bierma
UC, Irvine, Irvine, CA
Factors that influence thermal stability of proteins is still not
well understood, particularly in psychrophilic organisms.
Inferences about thermal adaptation can be made by
comparing the structures of protein orthologs from organisms
that live in different thermal environments. The Antarctic
toothfish, D. mawsoni, is a psychrophilic organism that lives at
temperatures which cause cold cataracts in other mesophilic
species, due to phase separation of the lens crystallins. The
crystallins are a highly conserved group of proteins that make
up the lenses of a wide variety of animals. Here we present
preliminary structural data on D. mawsoni γS1- and γS2crystallins and comparisons to γS-crystallins in mesophilic
organisms, .
Poster 026
Structural Characterization of the Complex between the
Transactivation Domain of p65 and TFIIH
Lauriane Lecoq; Luca Raiola; Philippe Chabot; Normand Cyr;
Geneviève Arseneault; James G. Omichinski
Département de Biochimie et Médecine Moléculaire,
Montréal, Canada
p65 is a member of NF-κB, a family of proteins that plays a
key role in immune response and cell survival. The
transactivation domain (TAD) of p65 interacts with the general
transcription factor TFIIH, and this interaction is essential for
the role of NF-κB in the immune response and HIV infection.
We have solved the NMR structure of the p65 in complex with
Poster 029
Chemo-enzymatic Synthetic Strategies to Aid in RNA
Structure and Dynamics Studies by NMR Spectroscopy
1
1
1
1
Owen Becette ; Regan Leblanc ; Bin Chen ; Luigi Alvarado ;
1
2
1
Andrew Longhini ; Cristoph Kreutz ; Kwaku Dayie
1
2
University of Maryland, College Park, MD; University of
Innsbruck, Innsbruck, Austria
Non-protein coding RNAs can undergo conformational
transitions in response to ligands to promote or repress
downstream gene expression. Although X-ray crystallographic
studies of such RNAs provide insight into ligand binding, NMR
spectroscopy is the only high resolution technique capable of
probing the highly dynamic unbound state. Here we present
site-selective labeling strategies and NMR methodologies to
study the structure and dynamics of ligand-free RNAs. The
combination of our selective labels with customized NMR
experiments alleviates problems of rapid relaxation and
Page 51
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
spectral crowding, thereby allowing us to investigate the
structure and dynamics of relatively large RNAs.
Poster 030
Saturation Transfer Difference (STD) NMR Studies of
Substrate Specificity for Sialyltransferases
Cheng-Yu Chen; Zhongwei Gao; Lu Meng; Lin Liu; Anthony
Prudden; Geert-Jan boons; Kelley W. Moremen;
James H. Prestegard
CCRC, University of Georgia, Athens, GA
Glycans produced by glycosyltransferase enzymes in
mammalian cells play critical roles in cell communication,
proliferation and development. Sialyltransferase, which
synthesizes the terminal sialic acid residues of glycans
belongs to a specific family of these enzymes. The diverse set
of linkages and acceptor specification catalyzed by
sialyltransferases contribute to the diverse glycan structures.
In this study, we examined the substrate specificities for the
enzyme ST6GAL1 and ST3GAL4 by using saturation transfer
difference NMR. The binding epitopes of both the donor,
CMP-Neu5Ac and the acceptor, Galb1,4GlcNAc-OMe
(LacNAc-OMe) was identified. Epitope mapping indicates a
different binding mode for these two enzymes. Enhanced STD
from donor suggests cooperative binding. A longer, branched
hepta-glycan was synthesized and evaluated for its binding to
the two enzymes.
Poster 031
NMR Visualization of the Water-Soluble and MembraneIntegrated Functional States of Anti-Apoptotic BCL-XL
1
1
1
Yong Yao ; Lynn Fujimoto ; Nathan Hirshman ; Antonella
2
2
1
Antignani ; Richard Youle ; Francesca Marassi
1
Sanford Burnham Medical Research Institute, La Jolla, CA;
2
National Institute of Health, Bethesda, MD
To understand how BCL-2 proteins employ their C-terminus to
associate with their partners and with membranes we have
used NMR spectroscopy to examine the structure and
function of BCL-XL, including its hydrophobic C-terminus. We
describe the conformations of two functional states of BCLXL: a water-soluble state and a membrane-integrated state,
each state is competent with respect to their ability to bind a
BH3 ligand. We show that the two states differ primarily with
respect to the conformation of the C-terminus, which interacts
with the BH3-binding pocket in the soluble form, and inserts
across the membrane bilayer in the membrane-associated
state. The NMR spectra of the two protein states yield singlesite resolution for direct detection of ligand binding or
conformational changes.
Poster 032
Covalently Circularized Nanodiscs for Structural and
Functional Studies of Membrane Proteins
1
1
1
Mahmoud Nasr ; Diego Baptista ; Thomas Raschle ; Franz
2
1
1
1
Hagn ; Sonja Studer ; Thomas Walz ; Gerhard Wagner
1
2
Harvard Medical School, Boston, MA; Technische
Universität München, Garching, Germany
Nanodiscs, unlike detergent, offer a more biologically relevant
environment to study membrane proteins using solution NMR.
The nanodisc size distribution remains a major obstacle for
detailed NMR structural determination. Also, a variable
number of membrane proteins can incorporate into each disc,
and result in a sample with a mixed population of membrane
proteins per nanodisc. Here we present a method to make
circularized nanodiscs using evolved sortase. We have
Page 52
created nanodiscs of different sizes and we were able to
confirm sortase reaction fidelity by mass spectrometry and
confirm the homogeneity by negative-stain EM. We will
present a comparison of NMR data for a membrane protein
incorporated in a circularized and a conventional nanodiscs.
Poster 033
Structural Features and Critical Roles of Cell Membrane
Fusion Protein Modules
Muzaddid Sarker; Tim Key; Jolene Read; Jan Rainey;
Roy Duncan
Dalhousie University, Halifax, Canada
The fusion-associated small transmembrane (FAST) proteins
are a unique family of cell membrane fusion proteins encoded
by the nonenveloped fusogenic reoviruses. Our NMR studies
reveal critical structure-function relationships of essential
FAST protein domains. The avian reovirus p10 ectodomain
contains a small, geometrically constrained, cystine noose.
The α-helical reptilian reovirus p14 FAST protein
transmembrane domain (TMD) is inherently flexible due to a
degree of curvature and exhibits unexpected interfacial
positioning of the hydrophobic and hydrophilic residues
including essential N-terminal β-branched residues and a
solvent-accessible cleft. The baboon reovirus p15 FAST
protein fusion-inducing lipid packing sensor (FLiPS)
comprises a novel type of helix-loop-helix conformation which
is functionally equivalent to, but structurally different from,
classical amphipathic helix or amphipathic lipid packing
sensor.
Poster 034
High-Resolution Characterization of Amyloid-β Oligomers
and Aggregation Using Solution- and Solid-State NMR
1
1
Samuel Kotler ; Jeffrey Brender ; Janarthanan
1
1
Krishnamoorthy ; Subramanian Vivekanandan ; Kazutoshi
1
2
1
Yamamoto ; Anirban Bhunia ; Ayyalusamy Ramamoorthy
1
University of Michigan, Ann Arbor, MI;
2
Bose Institute, Kolkata, India
The aggregation of amyloid-β is sensitive to a variety of
conditions that lead to diverse oligomeric states and these
may act as a potential platform for the propagation of
Alzheimer's disease. The nature and structure of Aβ
oligomers are poorly understood and seeking high-resolution
structural insights of Aβ oligomers has been a major challenge
to most techniques. Here, we use magic angle spinning
recoupling NMR experiments to obtain atomistic detail on a
non-frozen, non-isotopically labeled Aβ1-40 oligomer.
Futhermore, the self-assembly of the disordered Aβ oligomer
is monitored and compared to the assembly of Aβ fibrils using
time-course HSQC. This combinational approach utilizing
solution- and solid-state NMR provides atomic-level details on
Aβ aggregation.
Poster 035
NMR Spectroscopy of Encapsulated Proteins : Structural
Biology, Biophysics and Drug Discovery
Kathleen Valentine; Brian Fuglestad; Evan O'Brien; Bryan
Marques; Christine Jorge; Nathaniel Nucci; Matthew Stetz;
A. Joshua Wand
University of Pennsylvania, Philadelphia, PA
Solution NMR is a powerful biophysical and biochemical tool
through its ability to examine both the structure and dynamics
of macromolecules at atomic resolution. Conventional solution
NMR approaches are largely limited to examinations of
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
relatively small macromolecules, mostly due to the
consequences of slow rotational diffusion. Encapsulation of
macromolecules within the protective aqueous interior of
reverse micelles prepared in low viscosity fluids circumvents
many aspects of the “slow tumbling problem” and has been
successfully applied to proteins and nucleic acids ranging up
to 100 kDa. Several applications of the general strategy will
be presented. These examples highlight the characterization
of membrane-associated proteins, protein-ligand interactions
including a novel application in drug discovery, and
investigation of biophysical phenomena such as protein
hydration.
Poster 036
Examining the Surface Hydrophobicity Present Among
Human gS-Crystallin and the Cataract Variant G18V
Domarin Khago; Rachel W. Martin
Department of Chemistry, University of California, Irvine, CA
gS-crystallin is the main component expressed outside of the
human eye lens (present up to 450 mg/mL) that contributes to
organization of the lens fiber. To remain stable and retain high
refractive indices, gS-crystallin depends on its long-term
solubility. The G18V point mutation (gS-G18V) results in
decreased stability and increased aggregate formation. Selfaggregation can occur due to an increase in net hydrophobic
interactions, previously shown in human gD-crystallin. To
investigate the solubility change and aggregation between gSG18V and its wild type counterpart, we concentrate on the
structural differences of the two proteins once binding a
hydrophobic chemical probe by using a NMR spectroscopy.
Poster 037
2+
2+
Determination of Free Mg and Ca in Biological
31
Systems using P solution-state NMR at 8 °C and 25 °C
1
1, 2
1, 2
Natalia Kozlyuk ; Andrej Luptak ; Rachel W. Martin
1
Department of Chemistry University of California, Irvine, CA;
2
Molecular Biology and Biochemistry, Irvine, CA
2+
2+
Nucleic acids or some proteins require Mg and Ca to
properly function. Determining the free divalent cation
2+
2+
concentration of Mg and Ca in biomolecular NMR samples
is important to gain insight into the role the cations play, such
as the concentration required for the biomolecules to properly
31
fold and function. Using P NMR and a small chelator as a
probe (deoxycytidine diphosphate), our goal is to design a
2+
2+
method for determining the free Mg and Ca in NMR
samples. Also, our goal is to determine the free concentration
2+
2+
of Mg and Ca NMR samples containing the Dickerson
dodecamer or a calcium dependent crystallin in the presence
and absence of a membrane mimetic system (DLPC/DHPC)
at 8 °C and 25 °C.
Poster 038
Characterization of the Antifreeze Protein ApAFP752
1
1
2
2
Shelby Follett ; K. Wade Elliot ; Predrag Jevtic ; Daniel Levy ;
1
Krisztina Varga
1
University of Wyoming-Chemistry Department, Laramie, WY;
2
University of Wyoming-Molecular Biology Department,
Laramie, WY
Antifreeze proteins are an evolutionary response that
contributes to the freeze resistance of certain fish, insects,
bacteria, and plants. These proteins adsorb to an ice crystal
surface and restrict the growth within a certain temperature
range. The exact mechanism of growth inhibition is still not
fully understood, but with further knowledge these proteins
may have potential applications in fields ranging from
medicine to agriculture. ApAFP752 is an 8.9-kDa hyperactive
antifreeze protein found in the desert beetle Anatolica polita
and is proposed to have a β-helical secondary structure with a
flat ice-binding surface. The structural and functional
characterization of ApAFP752 is currently under investigation
through nuclear magnetic resonance (NMR) spectroscopy and
in vivo studies.
Poster 039
Structural Analysis and Control of the Peptide Backbone
Geometry in Collagen Model Peptides.
1
2
1
Anaïs Terrien ; Grégory Chaume ; Yves Jacquot ; Rodrigue
1
2
3
Marquand ; Thierry Brigaud ; Young Kee Kang ;
1
Emeric Miclet
1
2
Univ. Pierre et Marie Curie, Paris, France; Université de
3
Cergy Pontoise, Cergy Pontoise, France; Chungbuk
University, Cheongju, Chungbuk, South Korea
We have developed a method allowing the determination of
the local backbone conformation of Collagen Model Peptides
in solution. Triple helices in equilibrium with minor structures
have been analysed in details using both NMR and CD
spectroscopy. We have been further interested in the design
of
innovative
CMPs
incorporating
trifuormethylated
pseudoprolines. NMR studies and theoretical calculations
have been performed on small tripeptides and have shown
d
that trifluoromethyl C -substitutions of oxazolidine-based
pseudoprolines can strongly influence the peptide bond cistrans rotational barriers with only moderate effects on the
d
cis/trans population ratio. Moreover, the C -configuration can
be used to efficiently constrain the ring puckering which is of
prime importance for the formation of collagen triple helices.
Poster 040
Probing Enzyme Catalysis in Tryptophan Synthase with
17
O-Quadrupole Central Transition NMR
Robert P. Young; Bethany G. Caulkins; Michael F. Dunn;
Leonard J. Mueller
University of California, Riverside, CA
Oxygen NMR parameters are challenging to obtain, but
extremely sensitive probes of chemical state within enzyme
17
active sites. Here we report the use of O-quadrupole central
transition (QCT) NMR spectroscopy to interrogate chemical
mechanism in the 144 kDa, pyridoxal-5’-phosphate dependent
enzyme tryptophan synthase. By supplying L-serine enriched
in the carboxylic oxygen positions, we can test competing
models of protonation at this site as the enzyme-substrate
complex moves through two quasi-stable intermediate states.
Our results lend support to the potentially controversial
hypothesis that acid forms of the substrate play an important
role during catalysis, helping to direct reaction specificity.
Extracted isotropic chemical shifts, chemical shielding, and
quadrupolar product parameters are found to track DFT
cluster calculations of the active site.
Poster 041
The Core Template/Pseudoknot Domain of Vertebrate
Telomerase RNA is Structurally Conserved
Yaqiang Wang; Juli Feigon
University of California Los Angeles, Los Angeles, CA
Telomerase is a large ribonucleoprotein complex that is
essential for maintaining telomere length and chromosomal
stability. Among vertebrates, telomerase RNA contains two
conserved domains, the template/pseudoknot and CR4/5
Page 53
POSTERS
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
domains. Within the vertebrate pseudoknot, there are two
subdomains, P2ab and the minimal pseudoknot. We are
investigating the full-length TR pseudoknot in the model
vertebrate organism Oryzias latipes, which is the smallest TR
identified to date among vertebrate species. We have
determined the structure of P2ab, the secondary structure of
the minimal pseudoknot, and have identified an unexpected
domain in the full-length pseudoknot by NMR. Telomerase
activity assays confirm the importance of the unpredicted
domain. These results provide new insight into the essential
elements of the full-length pseudoknot for telomerase activity.
Poster 042
Analysis of Protein Dynamics in Macromolecular
Crowding Environment
1
1, 2
Hideyasu Okamura ; Takanori Kigawa
1
RIKEN Quantitative Biology Center (QBiC), Yokohama,
2
Japan; Tokyo Institute of Technology, Yokohama, Japan
In biological cellular environment, biomolecules are generally
surrounded by high concentrations of macromolecules, socalled “macromolecular crowding”. In order to elucidate the
effect of the macromolecular crowding on the biomolecular
structural dynamics, we have investigated in detail NMR
relaxation data of the model protein systems composed of
Villin protein at concentrations ranging from 0.1 mM (diluted)
to 32 mM (highly concentrated). By applying a newly
developed model-free analysis, we found that the relaxation
data could be explained by contributions of two rotational
motions: the faster one is induced by Brownian motion,
whereas the slower one by intermolecular interactions. The
latter becomes predominant at higher concentrations,
suggesting the important role of intermolecular interactions in
the biomolecular structural dynamics in the macromolecular
crowding.
Poster 043
Can Sparse RDCs Complement Sparse NMR Restraints in
Structural Studies of Large RNAs?
Gabriel Cornilescu; Allison Didychuk; Lauren Michael; Marco
Tonelli; David A. Brow; John L. Markley; Samuel E. Butcher
University of Wisconsin-Madison, Madison, WI
We studied a 92-nucleotide U4/U6 Spliceosomal RNA
Complex by NMR. Traditional ‘divide-and-conquer’ RNA
methods to assign its NMR spectra provided only a sparse set
of structural constraints due to spectral broadening and
overlap typical for its molecular size. In addition to SAXS, we
measured residual dipolar couplings (RDCs) in three
alignment media resulting in a sparse dataset (24 imino NH
and 10 base CH RDCs in each medium). While RDCs in the
different media were highly uncorrelated, the corresponding
alignment tensors proved to be largely linearly dependent.
Nevertheless, the RDCs in these media provided sufficient
structural restraining power (as assessed by jackknife and
Monte-Carlo analyses) complementary to SAXS and
traditional structural constraints to improve the NMR
structures locally and globally.
Poster 044
Characterization of Partially Disordered Delta Subunit of
RNA Polymerase from B. subtilis
Vojtech Kuban
Masaryk University, CEITEC, Brno, Czech Republic
RNA polymerases of gram-positive bacteria differ from well
described RNA polymerases of gram-negative bacteria in the
Page 54
presence of two additional subunits interacting with the core
enzyme, delta and epsilon. The studied delta subunit of
Bacillus subtilis consists of structured N-terminal domain
(structure has been solved) and disordered C-terminal
domain. NMR experimental data including chemical shifts,
residual dipolar couplings, and paramagnetic relaxation
enhancements were obtained previously in our laboratory on
the the delta subunit. These data were used to select a
representative sub-ensemble of the C-terminal domain from a
large explicit structural ensemble based on statistical coil
sampling. The final result showed propensities to adopt
different structural motives for the unstructured C-terminal
domain. Protocols for flexible-meccano and ASTEROIDS
software were used.
Poster 045
Calmodulin Capping of the N-terminus of PSD-95 Triggers
its Postsynaptic Release
1, 2
1
1
Yonghong Zhang ; Lucas Matt ; Tommaso Patriarchi ;
1
1
Johannes Hell ; James Ames
1
2
Univ. of Calif,Davis, Davis, CA; University of Texas-Pan
American, Edinburg, TX
As a central element of the postsynaptic architecture of
glutamatergic synapses, PSD-95 plays an important role in
synaptic plasticity. Ca2+ influx via postsynaptic receptors
induces release of PSD-95 from postsynaptic membranes.
We present NMR structural analysis of Ca2+/calmodulin
bound to PSD-95, which reveals Calmodulin collapses onto a
helical structure of PSD-95 N-terminus. This N-terminal
capping by Calmodulin blocks palmitoylation of Cys3 and
Cys5, which is required for postsynaptic PSD-95 targeting.
Calmodulin forms extensive hydrophobic contacts with Tyr12
of PSD-95. The Y12E mutant strongly impairs its binding to
Calmodulin and Ca2+-induced release of PSD-95 from
postsynaptic membrane. Our NMR structure and functional
data indicate that Calmodulin binding to PSD-95 serves to
block PSD-95 palmitoylation, and promotes Ca2+-induced
dissociation from postsynaptic membrane.
Poster 046
Dynamic Conformation of Z-DNA Binding Domain of PKRlike Protein Kinase (PKZ) Modulates Its
B-Z Transition Activity
Ae-Ree Lee; Joon-Hwa Lee
Gyeongsang National University, Jinju, South Korea
A protein kinase, PKZ, contains two left-handed Z-DNA
binding domains (Zα and Zβ). The Zα domain of PKZ from
gold fish (caZαPKZ) exhibits the unusual hydrogen bonding
interaction of K56 with the T0pC1 phosphate of dT(CG) 3 for
efficient Z-DNA binding affinity in contrast to other Z-DNA
binding proteins. In this study, we determined the solution
structure of the free caZαPKZ by multidimensional
heteronuclear NMR spectroscopy. We performed NMR
experiments on complexes of caZαPKZ with dT(CG) 3 and also
investigated the conformational changes of caZαPKZ induced
by increment of NaCl concentration. This study provides the
molecular basis for B–Z transition mechanism of caZαPKZ,
which is modulated by conformational dynamics of a key
tyrosine residue in the α3 helix.
POSTERS
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
Poster 047
Characterization of Interaction Between Flagellar Type III
ATPase FliI, Cap-Forming Protein FliD and Flagellar
Export Chaperone FliT
1, 2
1, 2
1
Paolo Rossi ; Nandish Khanra ; Babis Kalodimos
1
Center for Integrative Proteomics Research- Rutger,
2
Piscataway, NJ; Rutgers University, Piscataway, NJ
Bacterial flagella are the motility organs of gram-negative
bacteria. Construction of these systems begin via formation of
the main membrane-bound motor scaffold followed by
secretion of protein building blocks that extends the organelle
into the extracellular space. FliI is the 50 kDa soluble ATPase
protein of the flagellar export apparatus in Salmonella enterica
similar to F0-F1 ATPase. In vivo, FliI self-assembles into a
homo-hexamer export gate. FliT is the flagellar export
chaperone for the cap-forming protein FliD. The interaction
between FliT & FliI is required for the transport of FliD through
the secretion channel. The solution structure of FliI-FliT and
FliD-FliT complexes were determined. The structures,
biophysical essays and NMR titration data provide insights
into flagellar export process.
Poster 048
1
INTOXSY: A Method for Hydroxyl H Exchange Rate
Determination for Glycans in Natural Abundance
Marcos Battistel; Hugo Azurmendi; Daron Freedberg
Food and Drug Administration, Silver Spring, MD
1
Solvent exchange rate constants (kHD) for labile H’s are
useful for inferring hydrogen bonds (H-bonds), which are
essential for stabilizing higher order structures in biomolecules
and for substrate binding. H-bonds play an important role in
glycan structures as well, but have been undetectable until
recently. We present INTOXSY, a new experiment for
determining hydroxyl kHD for molecules in natural abundance.
The aim of our work is to determine hydroxyl group (OH) kHD
for glycans in water and use this information in conjunction
with molecular dynamic simulations to infer H-bonds. We
demonstrate that H-bonds donor and acceptor groups can be
inferred based on INTOXSY data vis-à-vis MD simulations for
β-cyclodextrin and sialyl Lewis X.
Poster 049
Structural Study of a Middle Domain of Arc Protein
2
1
3
Grace Royappa ; Jody Shimabukuro ; Keith Nakamatsu ;
4
1
Roland Riek ; Lei Wang
1
2
Hawaii Pacific University, Honolulu, HI; St Jude Children's
3
Research Hospital, Memphis, TN; Windward Community
4
College, Kaneohe, HI; ETH Zurich, Zurich, Switzerland
Synaptic plasticity is a molecular mechanism underlying
memory formation. Activity-regulated cytoskeleton-associated
protein (Arc) is an essential protein that mediates synaptic
plasticity, and it plays an important role in regulating longterm, but not short-term, memory formation. The structure of
Arc and how it interacts with binding partners in neurons
remain unclear. Solving the high-resolution structure of Arc
could help identify its interaction sites with binding partners
and understand how these interactions regulate synaptic
plasticity. We successfully expressed and purified a middle
domain of Arc protein and characterized its structure by using
solution-state NMR techniques. Here, we report its secondary
and tertiary structure.
Poster 050
Solution Structure of RING Domain of Doa10 and Its
Interaction with Ubc6
Hee-Chul Ahn; Myungbo Shim
Department of Pharmacy, Dongguk University, Goyang,
South Korea
Doa10, one of E3 ligases, is involved in ER-associated
degradation (ERAD). We present the solution structure of
RING domain of Doa10 and its interaction with Ubc6, an E2
enzyme of yeast by NMR spectroscopy. The overall structure
of Doa10 RING domain was very similar to other RING
domains, which is a compact and stable fold exhibiting an αβ
structure in cross brace manner. Two zinc atoms are
coordinated by 3 cysteines and one histidine in the amino acid
sequence of Cys-X2-Cys-X9-39-Cys-X1-3-His-X2-3-Cys-X2Cys-X4-48-Cys-X2-Cys. NMR spectroscopy with wild-type
and mutated Doa10 RING domain revealed its binding
interface to Ubc6, and in vitro ubiquitination assay supported
the relationship between the protein-protein interaction in
ERAD.
Poster 051
Single Base Lesions in DNA Alter Non-Exchangeable
Proton Chemical Shifts, NOE intensities, and DQFCOSY
Coupling Patterns Near Lesion Site
Stephen Kramer; Brianna Medrano; Chunling Cao; Aaron
Proctor; Chris Reynolds; Mallory Clark; Amy Terbrock; Juliano
de Oliveira Silveira; Gary A. Meints
Missouri State, Springfield, MO
Altered local conformational properties (local structure and
dynamics) in damaged DNAs have been suggested to assist
enzyme recognition and specificity.
2D solution NMR
techniques have been used to observe changes in nonexchangeable proton chemical shifts, NOE intensities, and
DQFCOSY coupling patterns due to the presence of several
single base lesions (uracil, 8-oxoguanine, 8-oxoadenine,
1,N6-ethenoadenine
and
3,N4-ethenocytosine
sites)
compared to a control DNA sequence. Peak modifications
are localized to the three nucleotide region associated with
most lesions, but more significant changes occur due to the
presence of an alkylated base. The results for an alkylated
base sequence are qualitatively supported by solid-state
deuterium NMR lineshapes.
The results suggest local
conformational rearrangement may play a role in recognition
by repair enzymes.
Poster 052
Structural and Functional Studies of the Carbohydrate
binding module StX (CBM64)
1
1
Bruna Medéia De Campos Ramos ; Mauricio Sforça ; Fabio
2
1
Marcio Squina ; Ana Carolina de Mattos Zeri
1
LNBio - National Laboratory of Biosciences, Campinas,
2
Brazil; CTBE - Laboratório Nacional de Ciência e Tecnologi,
Campinas, SP
In recent years, biofuels have attracted great interest as a
source of renewable energy owing to the growing global
demand for energy and limited natural resources. However,
the cost effective production of biofuels from plant biomass is
still a challenge. In this context, the study of carbohydratebinding modules (CBMs), involved in guiding the catalytic
domains of glycoside hydrolases to polysaccharides, is crucial
for enzyme development. Aiming at the structural and
functional characterization of novel CBMs involved in plant
Page 55
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
polysaccharide deconstruction, a CAZy database analysis
was performed and CBM family 64 was chosen owing to its
capacity to bind with high specificity to microcrystalline
cellulose. In this study, the three-dimensional structure of the
recombinant CBM64, named StX, was determined by NMR.
Poster 053
3D NMR Solution Structure of Acidocin B, a Circular
Bacteriocin Produced by Lactobacillus acidophilus M46
Jeella Z. Acedo; Marco J. van Belkum; Christopher T. Lohans;
Ryan Mckay; Mark Miskolzie; John C. Vederas
Chemistry - Univ. of Alberta, Edmonton, Canada
Acidocin B is a bacteriocin produced by Lactobacillus
acidophilus M46 and was originally reported to be a linear
peptide composed of 59 amino acids. A high sequence
similarity to a circular bacteriocin (gassericin A - Lactobacillus
gasseri LA39) suggested that acidocin B might in fact be
circular as well. Acidocin B was purified and its circular nature
confirmed by MALDI-TOF and MS/MS sequencing. The NMR
solution structure of acidocin B in SDS micelles was solved,
revealing four �-helices of similar length that are folded to
form a compact, globular bundle with a central pore.
Comparison of acidocin B with carnocyclin A (subgroup I
circular bacteriocin), revealed differences in the overall fold.
Poster 054
NMR Provides Critical Insight into the Cold Unfolded
State of Proteins
Natalie Stenzoski; Daniel Raleigh
SUNY-Stony Brook, Stony Brook, NY
Cold denaturation is a general feature of globular proteins, but
is hard to study because of the difficulty in populating the cold
unfolded state in buffer in the absence of added denaturants,
extremes of pH or encapsulation.
We have rationally
designed mutants of the C-terminal domain of L9 that allow
the cold denatured state ensemble (cold DSE) to be observed
using NMR at temperatures above zero Celsius. The cold
DSE is in slow exchange with the native state on the NMR
chemical shift time scale. Paramagnetic relaxation
enhancement measurements, performed using six separate
cysteine mutants with site-specific spin labels, reveal transient
long-range contacts in the DSE.
Poster 055
Enhanced and Efficient TOCSY Transfer by Time Variant
and Band Selective Mixing
Paul Coote; Gerhard Wagner; Haribabu Arthanari
Harvard Medical School, Boston, MA
Under a typical broadband TOCSY mixing pulse the chemical
shifts are effectively removed while effective/reduced Jcouplings allow magnetization to move throughout the spin
network. Here, we demonstrate that time-varying and band
selective mixing pulse can lead to enhance transfer efficiency
between certain sets of resonances. This technique can be
used to efficiently assign aromatic side chain carbons to the
protein backbone by maintaining specific J-couplings for part
of the mixing sequence and then switching to a different set of
resonances. We use of time-varying TOCSY pulses to
efficiently assign methyl carbons in AILV systems of a protein.
The time-varying scheme can significantly enhance the crucial
"methyl-to-alpha-carbon" transfer step and will make a
significant impact in assigning methyl resonances of proteins.
Page 56
Poster 056
Dissecting the Structure and Function of the Three KH
RNA-binding Modules of hnRNP E1
Yang Li
MUSC, Charleston, SC
Comparative dynamics by NMR relaxation measurements
reveal KH1 homodimers, KH3 monomers and a KH1-KH2
platform in solution. A solution structure of a KH1 homodimer
was determined using an RDC-restrained Rosetta fold-anddock protocol. KH-KH2 has ca. 140 amino acids, we obtained
its solution structure by using sparse NMR restraints. We
used NMR titrations to characterize the interaction of
individual KH1 and KH3 as well as tandem KH2 domains of
hnRNP E1 with C-rich nucleic acids. We found that the three
KH domains have distinct binding affinities for the C-rich
oligonucleotide sequences.
Poster 057
Calcium Triggered Reversal of Calmodulin Bound to the
IQ Motif of the Neuronal Voltage-Dependent Sodium
Channel NaV1.2
C. Andrew Fowler; Mark Miller; Liam Hovey; Kristin Tefft;
Liping Yu; Madeline Shea
University of Iowa, Iowa City, IA
Calcium regulates human NaV1.2 via interactions with
calmodulin (CaM). Equilibrium dissociation measurements of
CaM binding to WT and mutant NaV1.2 IQ motif peptide (IQp)
suggest that although WT IQp binds CaM with similar affinity
with and without calcium, the interaction is via a different
2+
mechanism. We solved the solution structure of the (Ca )CaM C-terminal domain bound to NaV1.2 IQp (2M5E) and
compared it to the previous structure of the calcium free
2+
complex (2KXW). Strikingly, IQp binds (Ca )-CaM in the
opposite orientation compared with apo CaM. This first ever
pair of structures for CaM binding to the same sodium channel
peptide in the free and calcium bound states suggests
possible mechanisms by which CaM modulates NaV1.2
function.
Poster 058
Incorporation of the cyt b5 – cyt P450 Complex in
Nanodiscs Characterized by Solution NMR
1
1
2
Meng Zhang ; Rui Huang ; Rose Ackermann ; Sang-Choul
3
3
2
Im ; Lucy Waskell ; Anna Schwendeman ; Ayyalusamy
1
Ramamoorthy
1
Department of Chemistry, U of Michigan, Ann Arbor, MI;
2
Department of Medicinal Chemistry, U of Michigan, Ann
3
Arbor, MI; Dept of Anesthesiology, U of Michigan,
Ann Arbor, MI
Cytochrome P450s (P450s) are a ubiquitous superfamily of
enzymes responsible for the metabolism of a dazzling array of
substances, including over 75% of the marketed drugs.
Mammalian P450s are mostly located on the endoplasmic
reticulum membrane. Their structure and function have been
reported to be closely related to the membrane environment.
In this study, we introduce a modified nanodisc for the study
of cyt b5 – P450 interactions, which eliminates detergents
from the membrane mimetic. Successful incorporation of both
proteins on the same side of the nanodisc and formation of
the productive complexes are characterized by solution NMR.
Our study also suggests stronger binding between the two
proteins in nanodiscs compared to in bicelles.
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
Poster 059
Conformational Diversity of Fags1, an Allergenic Protein
of PR-10 Class, Characterized by NMR Spectroscopy and
Its Impact on Protein-Ligand Binding
1
2
1
Adolfo Moraes ; Claudia Asam ; Aline Batista ; Fabio
1
2
2
Almeida ; Michael Wallner ; Fátima Ferreira ;
1
Ana Paula Valente
1
Federal University of Rio de Janeiro, Rio De Janeiro, Brazil;
2
University of Salzburg, Salzburg, Austria
In this work we obtained the solution NMR structure of Fag s
1, a allergenic protein found in Fagales Sylvatica tree pollen.
We also characterized the molecular dynamics of Fag s 1 free
15
and bound to dehydroergosterol (DHE) using different Nrelaxation experiments. The structure of Fag s 1 is composed
by seven beta-strands, three alfa-helix and a big hydrophobic
cavity.
In many residues, contribution of conformation
exchange between the native and a less populated state on
15
R2 relaxation rate was identified. Analyzing N-CT-CPMG-R2
experiments using solutions of Bloch-MacConnel equation, we
characterized kinetically, structurally and thermodynamically
the less populated state of free Fag s 1 and correlated this
conformation with the DHE-bound state of Fag s 1.
Poster 060
Structural Aspects of Tt28: Diversity in the Folding of
Alpha-Toxins Confirmed by NMR Spectroscopy
David Flores Solis; Federico Del Rio-Portilla
Instituto de Química UNAM, México, Mexico
Scorpion toxins are proteins with activity against ion channels
on living cells. The three-dimensional structures of alphatoxins are known for their particular structural motif. The
recently solved structures by NMR spectroscopy of Tt2b and
Ts16 have been proven to exhibit a new type of folding, which
makes it difficult to include them in any alpha-toxin subfamily.
Previously Tt28, from Tityus trivittatus, was classified into a
new alpha toxin subfamily based on its similarity with alphatoxins. Ts16 and Tt2b share the highest identity with Tt28. In
this work we explore the structural features of the
recombinantly produced GS-Tt28. We determined its folding
by NMR as well as the specific connectivity of its disulfide
bonding by enzymatic reactions and MALDI-TOF data
analysis.
Poster 061
Mapping ZapA residues, Involved on Its Interaction with
FtsZ, on a ZapA-FtsZ Docking Complex
1
2
Maria Luiza Caldas Nogueira ; Mauricio Luis Sforça ; Paulo
2
2
Sergio Lopes Oliveira ; Rodrigo Vargas Honorato ; Glenn F
3
4
King ; Frederico José Gueiros-Filho ;
2
Ana Carolina de Mattos Zeri
1
2
Unicamp, Campinas, SP, Brazil; Brazilian Biosciences
3
National Laboratory, Campinas, SP, Brazil; IMB, The
University of Queensland, Brisbane/St Lucia, QLD, Australia;
4
Departamento de Bioquímica, IQ, USP,
São Paulo, SP, Brazil
In rod-shaped bacteria, the FtsZ protein assembles into a Z
ring structure, the main component of the divisome1. It is a
scaffold for assembly of the other divisomal proteins, which
modulates the septum formation. The ZapA protein is a
positive modulator that assists the bundling of FtsZ polymers.
ZapA promotes lateral association of FtsZ filaments and thus
helps formation of a continuous Z ring from relatively short
FtsZ polymers. Despite its important role in cell division, the
molecular details of ZapA-FtsZ’s interaction FtsZ are
unknown. Here we used NMR to solve the solution structure
of the ZapA dimer, to identify ZapA residues involved on its
interaction with FtsZ and mapped it on a docking model for
the FtsZ-ZapA complex.
Poster 062
Structural Analysis of Human Purinergic Receptor P2X7
by NMR
1, 2
Dinarte Neto Moreira Ferreira ; Viviane Medeiros Oliveira
1
2
1
Valença ; Luiz Anastácio Alves ; Mônica Santos De Freitas
1
2
UFRJ, Rio De Janeiro, Brazil; Oswaldo Cruz Foundation,
Rio de Janeiro, Brazil
The present work has the goal to study the structure of the
P2X7 human receptor that belongs to the purinergic cation
selective receptors family that are activated by extracellular
ATP. This receptor has low ATP affinity and plays an
important role in inflammation processes by , neurological
functions and neoplasie. The hP2X7R has raised up as a
potential target for drug development for the treatment of
several diseases such as rheumatoid arthritis and neutopathic
pain that has attracted the attention of pharmaceutical
industry.
The perspectives of this work is to contribute to a
better understanding about the functioning of the hP2X7R
supported by structural features to open new pathways to
allow the development of new therapeutic approaches related
to this receptor.
Poster 063
S-Nitrosylation Induces Structural Changes in the
Cytoplasmic Rhodanese Domain of the Integral
Membrane Protein YgaP from E. coli
1
2
3
Cedric Eichmann ; Christos Tzitzilonis ; Tomohiro Nakamura ;
3
1
Stuart A. Lipton ; Roland Riek
1
2
ETH Zurich, Zurich, Switzerland; Structural Biology
3
Laboratory, The Salk Institute, La Jolla, CA; SanfordBurnham Medical Research Institute, La Jolla, CA
The α-helical integral membrane protein YgaP from
Escherichia coli with its cytoplasmic rhodanese domain is a
sulfurtransferase. The enzymatic activity of several
rhodaneses is inhibited by the covalent attachment of nitric
oxide (NO) to the cysteine thiol (S-nitrosylation). Here, we
report using a NO-biotin switch assay and NMR spectroscopy
that NO reacts with YgaP by S-nitrosylating its rhodanese
domain at the catalytic Cys-63, which causes widespread
conformational changes within the rhodanese domain.
Overexpression of the rhodanese domain alone induces
stress-elevated production of NO resulting in an expression
time dependent percentage of S-nitrosylated rhodanese
compared to the native form. These findings provide insights
into structural changes of the cytoplasmic rhodanese domain
of YgaP triggered by nitrosative stress.
Poster 064
Expression and Characterization of an Isotopically
Labeled Scytodes Venom Peptide
Lisa Muñoz; Nikolaus M. Loening
Lewis & Clark College, Portland, OR
Venomous spiders produce a cocktail of proteins and peptides
optimized towards subduing prey. Many venom peptides
target neuronal ion channels, and are of interest for their
potential pharmaceutical and agricultural applications. In this
Page 57
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
work we detail our progress in expressing and characterizing
SYTXD_7, a 32 residue peptide identified from the genus
Scytodes (the spitting spiders). This peptide contains six
cysteines, and is likely to contain the inhibitor cystine knot
(ICK) structural motif that is common to many cysteine-rich
venom peptides. To recombinantly express enough correctly
folded SYTXD_7 in E. coli for structural and functional
characterization, we have adopted a fusion protein system
with a periplasmic tag and have optimized our expression
15
13
protocol for cost-effective N/ C labeling.
Poster 065
Direct Interactions between an Aromatic Acyl Substrate
and the Peptidyl Carrier Protien, PltL
Matt J. Jaremko; D. John Lee; Michael D. Burkart
UCSD, La Jolla, CA
Carrier proteins regulate the biosynthesis of fatty acids,
polyketides,
and
non-ribosomal
peptides,
essential
components to all forms of life. Substrate sequestration and
protection has been reported in both fatty acid and polyketide
carrier proteins, but currently, there is no evidence in nonribosomal peptide carrier proteins (PCPs). Here we report
direct interactions between the pyoluteorin PCP, PltL, and a
unique pyrrole acyl substrate. NMR analysis of pyrrole and
intermediate mimetics attached to PltL revealed interactions in
residues of helix II and III. Furthermore, the solution NMR
structure of PltL with attached pyrrole was determined. This is
the first report of substrate interaction with a PCP, illustrating
the importance of biosynthetic regulation in this family of
carrier proteins.
Poster 066
Single Spin Inversion by J-driven Selective Cross
1
1
Polarization with Application to Measurement of H- H
Couplings
1
1
2
Ben Crane ; Sara Marquez ; Luke Arbogast ; Ananya
1
1
Majumdar ; Joel R Tolman
1
2
The Johns Hopkins University, Baltimore, Maryland; NISTIBBR, Rockville, MD
We have undertaken investigations of a new J-driven
selective inversion technique. This new pulse scheme, based
on established cross polarization methods, shortens total
inversion element length by roughly 2/3 for amide proton
inversion and simplifies implementation. Implementation
requires application of on resonance Hartman-Hahn matched
fields with the additional constraint of satisfying specific
solutions for contact time and field strength based on the Jcoupling of the target spin. Furthermore, comparisons of
theoretical simulations and experimental tests are in general
agreement, prompting ongoing efforts to apply this method to
1
1
measuring H- H couplings with future ambitions for
biomolecular applications. This ability to selectively decouple
or recouple specific spin coupling interactions has implications
for general pulse sequence design.
Poster 067
Deciphering GPCR Signal Transduction through NMR
Structure and Dynamics Studies
1
2
3
Joshua Ziarek ; Franz Hagn ; Andreas Plückthun ;
1
Gerhard Wagner
1
2
Harvard Medical School, Boston, MA; Technical University
3
of Munich, Munich, Germany; University of Zurich, Zurich,
Switzerland
Page 58
G protein-coupled receptors (GPCRs) are highly dynamic –
possessing a complex energy landscape rather than a binary,
‘on or off’, activation state. Even in the absence of ligand,
receptors exhibit basal activity by sampling conformations
consistent with downstream signaling. Although numerous
crystal structures have been determined in recent years,
these static representations reveal little on the dynamics of
ligand-binding and signal transduction. Production of
isotopically-labeled neurotensin receptor (NTR1) in E. coli
uniquely positions our lab to conduct a thorough NMR
exploration of GPCR conformational space. We are currently
probing backbone amide and side-chain methyl dynamics of
agonist- and antagonist-bound receptor. A complete picture of
GPCR dynamics will be drawn by combining NMR relaxation
measurements with crystal structures and MD simulations.
Poster 068
13
Assignment of Sparse C Alanine Methyl Resonances in
Hsp90 Proteins using RDCs, PCSs, and NOEs
1
1
2
Kari Pederson ; Laura Morris ; Daniel Elnatan ; Laura
2
3
3
2
Lavery ; Li-Chung Ma ; Gaetano Montelione ; David Agard ;
1
James Prestegard
1
2
University of Georgia, Athens, GA; University of California,
3
San Francisco, CA; Rutgers University, Piscataway, NJ
Hsp90 proteins undergo large conformational changes in their
role as molecular chaperones during protein folding. Studying
these conformational changes and interactions with clients by
NMR is currently prohibited by the size of Hsp90 proteins and
limitations of NMR resonance assignment strategies. Using a
13
single C-methyl labeled amino acid reduces the number of
cross peaks and improves resolution in multi-dimensional
experiments with additional advantages from methyl TROSY
effects. However, new assignment strategies are necessary.
In systems with an existing structure it is possible to use
RDCs, PCSs, and NOEs to assist with assignment of
resonances. The method is illustrated with the human
mitochondrial (TRAP1) and the bacterial (HtpG) Hsp90
proteins for which only the alanine methyl groups have been
1
13
H- C labeled.
Poster 069
NMR Studies of Membrane-Anchored STIM Proteins using
Nanodisc-Based Lipid Bilayer
1
1
2
Tadateru Nishikawa ; Le Zheng ; Peter B. Stathopulos ;
3
1
Mohammad T. Mazhab-Jafari ; Mitsu Ikura
1
Princess Margaret Cancer Centre, UHN, Toronto, ON;
2
3
University of Western Ontario, London, ON; Hospital for Sick
Children, Toronto, ON
2+
STIM1 is a Ca sensor protein localized on the endoplasmic
2+
reticulum (ER) membrane. When the Ca is depleted from
the ER lumen, the signal is initiated by STIM1 and transduced
2+
to plasma membrane-resident Ca channels, Orai1. The
2+
process is coupled with Ca depletion-dependent unfolding
and oligomerizaiton of the protein. It is however, the structural
detail and the relationship to stability and unfolding on the ER
membrane still remain elusive. To investigate this process
under a membrane mimetic condition, we constructed
nanodisc tethered STIM1 luminal domain. Nanodiscs are
stable monodisperse discodial phospholipid bilayers bundled
with an engineered amphiphilichelical membrane scaffolding
proteins (MSP) developed by Sligar and coworkers (Univ. of
Illinois). Here, we will present this methodology and our initial
NMR results.
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
Poster 070
Spin Diffusion Editing for
High Order Structure of Antibodies
1
1
2
Joshua Franks ; John Glushka ; Michael Jones ; David H.
1
1
2
Live ; James Prestegard ; Qin Zou
1
University of Georgia/CCRC, Athens, GA;
2
Pfizer Inc., St. Louis, MO
Proteins, including antibodies, are increasingly being used as
therapeutic and diagnostic agents. Assuring the quality and
stability of preparations is challenging in that changes in high
order structure, in addition to composition, must be monitored.
One dimensional proton NMR methods are capable of rapidly
assessing both composition and high order structure, but
interfering signals from high concentrations of excipient used
in typical formulations must be suppressed.
Here we
demonstrate a combination of spin diffusion editing,
translational diffusion editing and spin relaxation editing to
achieve these goals on a monoclonal antibody sample.
Excipient signals are suppressed by more than a factor of 500
and partial disorder of protein segments on a decrease in pH
can be seen.
BIOMOLECULES IN THE SOLID STATE
071 - 117
Poster 071
Peptide Orientation in Membranes is Governed by
Hydrophobic Matching and Lipid Spontaneous Curvature
1
1
Erik Strandberg ; Jonathan Zerweck ; Ariadna Grau2
3
1
Campistany ; Marie-Claude Gagnon ; Parvesh Wadhwani ;
1
1
3
Johannes Reichert ; Jochen Bürck ; Jean-Francois Paquin ;
3
2
1
Michèle Auger ; Francesc Rabanal ; Anne S. Ulrich
1
Karlsruhe Inst. of Technology, Karlsruhe, Germany;
2
3
Universitat de Barcelona, Barcelona, Spain; Université
Laval, Québec City, Canada
Membrane-active peptides have a biological function related
to their structure and orientation in the membrane. Using
solid-state NMR to study the orientation of peptides in model
membranes with different properties, we found that the
hydrophobic matching concept applies to both hydrophobic
and cationic amphipathic membrane-spanning peptides. The
insertion depends strongly on the lipid spontaneous curvature.
α-helical antimicrobial peptides are always staying flat on the
membrane surface in lipids with negative spontaneous
curvature, like PE lipids, while in lipids with positive
spontaneous curvature, like lyso-lipids, peptides can get tilted
or inserted. This spontaneous curvature concept also applies
to large β-barrel outer membrane proteins, and seems to be a
biophysical feature of membranes, valid for any peptide or
protein bound to membranes.
Poster 072
An Efficient Solid State NMR Method for Characterisation
of 14N Sites by Indirect Detection in Biological Samples
1
2
1
James Jarvis ; Ibraheem Haies ; Marina Carravetta ;
1
Philip Williamson
1
2
University of Southampton, Southampton, UK; University of
Mosul, Mosul, Iraq
Nitrogen is highly abundant in nature, but the naturally
abundant 14N isotope is not routinely studied by NMR, since it
is a spin-1 isotope that frequently exhibits a large quadrupolar
interaction.
We report on a novel method for indirect detection of 14N via
spin-1/2 nuclei. This method is sensitive and robust in
recording 13C/14N and 1H/14N correlation spectra of small
biological molecules. Furthermore, we present results of this
approach applied to a microcrystalline protein, GB3. We
demonstrate that isotropic second order quadrupole shifts
may be derived from assigned 14N sites, and are highly
dependent on the secondary structure of the protein at the
14N site, providing a novel route to the structural
characterization of proteins via the 14N quadrupolar coupling.
Poster 073
1
Ribosomal Complexes by H-detected Ultra-Fast MAS
Solid-State NMR
1
2
3
Emeline Barbet-Massin ; Eli van der Sluis ; Chih-Ting Huang ;
4
3
2
Venita Daebel ; Shang-Te Danny Hsu ; Roland Beckmann ;
1
Bernd Reif
1
2
Technical Universität München, Garching, Germany; Gene
Center, Ludwig-Maximilians-Universität, Munich, Germany;
3
4
Academia Sinica, Taipei, Taiwan; Bruker BioSpin GmbH,
Rheinstetten, Germany
We present first MAS solid-state NMR data on ribosomal
complexes that employ proton detection and ultra-fast MAS.
In particular, we focus of the ribosome-binding domain of
Trigger Factor (TF-RBD) which interacts with the 50S subunit
of the ribosome. Our results open new perspectives for the
study of large and dynamic ribosomal complexes for which
atomic-level structural characterization remains a challenge,
especially for non-crystalline ribosome nascent chains
complexes.
Poster 074
Transient Compensation in Symmetry-Based Recoupling
1
2
1
Johannes Wittmann ; Kazuyuki Takeda ; Beat Meier ;
1
Matthias Ernst
1
2
ETH Zurich, Zurich, Switzerland; Kyoto University,
Kyoto, Japan
Pulse transients, i.e. deviations of the rf field amplitude and
phase from the desired ideal shape, can have a severe impact
on the performance of multiple-pulse sequences in NMR.
Here, we show how transient-compensated pulses, which are
calculated by linear response theory, can be applied as basic
elements inside symmetry-based sequences, like the doublequantum recoupling sequence POST-C7. Based on a Floquet
analysis we propose modifications of the basic element
containing amplitude shaped pulses, which lead to high
double-quantum scaling factors with simultaneous chemicalshift suppression. We show, that the application of transientcompensation leads to a high reproducibility between different
experimental setups, especially, if small dipolar couplings
shall be determined.
Poster 075
14
High Resolution Overtone N NMR
Ibraheem Haies; James Jarvis; Ilya Kuprov; Philip T.F.
Williamson; Marina Carravetta
University of Southampton, Southampton, UK
14
There are two reasons why the overtone N NMR application
is currently limited: (1) The weak efficiency of the overtone
excitation. (2) Higher order quadrupolar coupling terms are
responsible for the residual linewidth of the peak
Here we present experimental data to address both of the
1
limitations above. (1) Polarization transfer techniques from H
Page 59
POSTERS
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
14
to the N overtone are used to enhance the overtone signal,
using cross polarization methods and symmetry-based Rsequences. We observe a signal enhancement of 6.5 and 2
when cross polarization methods and symmetry-based Rsequences are used respectively. (2) We present data
obtained by use of DOR (double rotation), which narrows the
14
linewidth of the N overtone transition.
Poster 076
19
A Knot in the Membrane: Insights from Solid State FNMR into How Cyclotides Interact with Membranes
1
2
2
Stephan Grage ; Olivier Cheneval ; Sonia Henriques ; David
2
3
3
1
Craik ; Pavel Mykhailiuk ; Igor Komarov ; Anne Ulrich
1
Karlsruhe Institute of Technology, Karlsruhe, Germany;
2
3
University of Queensland, Brisbane, Australia; National
Taras Shevchenko University, Kyiv, Ukraine
The cyclotide kalata B1 possesses an extremely stable
structure and many pharmaceutically highly relevant activities,
which involve its interaction with cell membranes. Getting
insight into this interaction of cyclotides with lipid bilayers was
the aim of our study. To this end we determined the
19
orientation of kalata B1 in lipid bilayers using solid state F19
NMR on oriented bilayers. For F-NMR, the protein was
labeled with the conformationally restricted amino acid CF3Bpg, which presents a direct probe for peptide backbone
orientation, in four different positions. Combining all
orientation constraints, an alignment of kalata B1 was found
which matches the amphiphilic character of this protein, and
which is supports previous accounts on the interaction of
kalata B1 with specific lipid headgroups.
Poster 077
Probing a Cell-Embedded Megadalton Protein Complex
by DNP-supported Solid-State NMR
Mohammed Kaplan
Universiteit Utrecht, Utrecht, Netherlands
Studying biomolecules at atomic-resolution in their native
environment is the ultimate aim of structural biology. Here, we
investigated the bacterial type IV secretion system core
complex (T4SScc), a one megadalton protein machine
consisting of 14 copies of 3 proteins (VirB7, VirB9 and VirB10)
to validate a structural model generated by combining in-vitro
and in-silico data. Using a combination of dedicated labeling
schemes, cellular ssNMR and Dynamic Nuclear Polarization
(DNP) allowed us to directly examine the validity of the
structural model of the membrane-associated T4SScc
complex in a cellular setting.
Our results indicate that T4SScc is well folded in the cellular
setting revealing protein regions that so far remained elusive
for in-vitro studies.
Poster 078
C CPMAS NMR Study of the Effect of Parity on Rat
Uterine Collagen Structure and Dynamics
1
2
1, 3
Basant Dhital ; Keith Downing ; Gregory Boutis
1
2
CUNY Graduate Center, New York, ; Montefiore, Albert
3
Einstein College of Medicine, Bronx, NY; Brooklyn College of
CUNY, Brooklyn, NY
Pelvic organ prolapse is a common condition affecting up to
half of the female population of United States over the age of
50 with parity being the largest risk factor. Previous studies
indicate that during pregnancy, remodeling of the pelvic floor
occurs causing alteration in the composition and organization
13
Page 60
of the extracellular matrix of which collagen is major
component. The dynamical and structural changes in
Sprague-Dawley rat uterine collagen were studied by 13C
CPMAS relaxation and chemical shift measurements. Despite
trauma to the tissue following pregnancy and birth, no
significant differences were observed in structure and
dynamics of collagen across rats following 1 pregnancy (2
weeks or 2 days postpartum), and in multiparous rats
compared to virgin rats.
Poster 079
A Polymer Composite Armor for Potatoes: Molecular
Insights from Solid-State NMR
1
2
1
Subhasish Chatterjee ; Chanh V. Phan ; Keyvan Dastmalchi ;
3
1
1
1
Boris Itin ; Linda Kallash ; Qing Cai ; Wenlin Huang ; Olga
4
4
4
1
Serra ; Marisa Molinas ; Mercè Figueras ; Ruth E. Stark
1
2
City University of New York, New York, NY; CUNY Hostos
3
Community College, Bronx, NY; New York Structural Biology
4
Center, New York, NY; University of Girona, Girona, Spain
The cultivation, storage, and marketing of potato tubers
require protection by a periderm comprised of waxes and
suberin, an aliphatic-aromatic biopolyester deposited on a
supporting polysaccharide cell-wall matrix. Differences in
suberin macromolecular structure and dynamics likely account
for the differing postharvest shelf life of potato cultivars, but
the insoluble, amorphous, heterogeneous periderm polymer
composite presents investigative challenges. Quantitative
13
DPMAS and multiple-CPMAS C NMR serve to evaluate
hydrophilic-hydrophobic balance and crosslink capabilities in
potato periderms: for nominally identical samples, differently
russeted and RNAi-silenced cultivars, native vs. woundhealing periderms. 2D DARR and related experiments on
wound periderms can monitor the development of a
hydrophobic barrier during tissue healing.
DNP shows
promise for signal enhancement, both overall and for
particular cell-wall components.
Poster 080
Amyloid Proteins Studied by Solid State NMR
Spectroscopy at High Sensitivity
1, 3
1
1
Henrike Heise ; Lothar Gremer ; Wolfgang Hoyer ;
1, 2
1
1, 3
Henrik Müller ; Ewa Mirecka ; Timo Piechatzek ;
1, 3
Franziska Weirich
1
Heinrich Heine Universität Düsseldorf, Düsseldorf, Germany;
2
3
University of Oxford, Oxford, UK; Forschungszentrum Jülich,
Jülich, Germany
Amyloid fibrils of recombinantly expressed IAPP were
investigated by MAS NMR spectroscopy with and without
DNP enhancement. Solid-state NMR signals were observed,
and site-specific assignments could be obtained for all
residues. The N-terminal loop seems extremely well ordered,
and secondary chemical shifts are indicative of 2 - 4 beta
strands in the C-terminal part. Signal enhancement by DNP
was successful.
Further, we investigate full-length recombinant ovine
recombinant PrP-amyloid seeded with brain derived prions.
We report preliminary site-specific resonance assignments
and compare results from different seeding protocols. Our
data indicate a semi-flexibile N terminus and a distinct beta
sheet core C terminal of residue ∼155.
POSTERS
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
Poster 081
Structure and Membrane Interaction of Orb2A
1
1
1
Maria Conrad Soria ; Alexander Falk ; Silvia Cervantes ;
2
1
1
Rachel Service ; Thalia Bajakian ; Ansgar Siemer
1
2
U. of Southern California, Los Angeles, CA; Eastern New
Mexico University, Portales, NM
Orb2 is a protein which forms amyloid-like aggregates
essential for long term memory formation in Drosophila
melanogaster. We sought to understand the role of one
isoform, Orb2A, in memory regulation by studying its
structure. Orb2A has a unique N-terminal domain, which
contains an amphipathic sequence that may interact with
membranes. Electron microscopy was used to visualize fibrils
of Orb2A, which were then studied in greater detail using
ssNMR with static selective and dynamic selective
techniques. Circular dichroism and electron paramagnetic
resonance were used to analyze changes in the structure of
Orb2A upon interaction with membranes. From these studies
we will begin to obtain the structural information necessary to
propose a mechanism for Orb2A amyloid fibril formation.
Poster 082
Solid-state NMR on Glutamine-Rich Functional and
Pathological Amyloids
Silvia Cervantes Cortes; Maria Conrad Soria; Alexander Falk;
Thalia Bajakian; Rachel Service; J Mario Isas; Ralf Langen;
Ansgar B Siemer
University of Southern California, Los Angeles, CA
Glutamine and asparagine rich proteins have the ability to
form amyloid fibrils. Some of these amyloids occur in
pathological contexts as for example the fibrils formed by the
protein huntingtin found in Huntington’s Disease (HD). Other
amyloid fibrils can have positive functions, for example the
glutamine-rich amyloid forming CPEB protein Orb2, which is a
key regulator of long-term memory in Drosophila. However,
the origin of amyloid toxicity on the one hand and the
mechanism of functional amyloids on the other is not known.
We will present solid-state NMR and EPR spectra on both
Orb2 and exon-1 of huntingtin. The comparison of the fibrils
formed by these two proteins is an important step towards
understanding pathological and functional amyloids alike.
Poster 083
Optimal Conditions for Proton Detection at 40 kHz MAS
Applied to Membrane Proteins in Native Lipid
Environments
1
1
1
Andrew Nieuwkoop ; Anja Voreck ; Daniel Stöppler ; Trent
1
1
1
2
Franks ; Umit Akbey ; Anne Diehl ; Peter Hegemann ;
3
3
1
Lyndon Emsley ; Guido Pintacuda ; Hartmut Oschkinat
1
Leibniz-Institut fuer Molekulare Pharmakologie, Berlin,
2
3
Germany; Humboldt University, Berlin, Germany; CNRS ENS Lyon, Lyon, France
The optimal conditions for proton detection at 40 kHz magicangle-spinning were investigated through the use of 1.3 and
1.9 mm probes and samples of microcrystalline SH3. Backexchange at 60% 1H2O was determined to be the best
compromise between sensitivity and resolution at 40 kHz
MAS. This condition was then applied to two membrane
protein preparations in native lipids: the ABC-transporter
ArtMP and the light-sensitive proton pump bacteriorhodopsin.
Poster 084
Dramatic Four-Fold Signal Enhancement Obtained by
1
15
using Free Radicals and Repetitive H- N Cross-
Polarization at Low RF Amplitudes for Oriented
Membrane Proteins
Sophie Koroloff; Deanna Tesch; Alexander A. Nevzorov
North Carolina State University, Raleigh, NC
Oriented-Sample Solid-State NMR (OS-NMR) provides
structural and dynamic information of membrane proteins
(MPs) under nearly physiological conditions. However, the
limited amount of protein considerably lengthens the
experimental time. In addition, the use of high-power
radiofrequency (RF) B1 field can lead to sample heating
and/or decrease the cross-polarization (CP) efficiency.
After optimizing the repetitive cross-polarization (REP-CP)
sequence at 19 kHz RF field, a signal gain of 60% was
obtained when compared to the widely used CP-MOIST
sequence at 50 kHz. By combining these results with the fast
T1Z paramagnetic relaxation (0.6 sec vs 6 sec) induced by the
5-doxyl stearic acid radical, we achieved a dramatic 15N
signal enhancement per unit time of more than four-fold
relative to CP-MOIST.
Poster 085
Proton-Detected Solid-State NMR Experiments under
Ultrafast MAS
1
2
1
Rongchun Zhang ; Manoj Pandey ; Joshua Damron ; Yusuke
2, 3
1
Nishiyama ; Ayyalusamy Ramamoorthy
1
2
University of Michigan, Ann Arbor, MI; RIKEN CLST-JEOL
3
Collaboration Center, Yokohama, Japan; JEOL Ltd.,
Tokyo, Japan
The development of ultrafast MAS technology has boosted up
a realm of proton-detected solid-state NMR methods due to
the attractiveness of high proton resolution as well as the
enhanced signal-to-noise ratio. In this presentation, we report
recently developed proton-detected multidimensional solidstate NMR methods for studies under ultrafast MAS
conditions, including the phase cycling schemes for fp-RFDR
1
1
in 2D H/ H chemical shift correlation, a proton-detected
separated-local-field NMR, and a 3D proton single
quantum/double quantum/single quantum (SQ/DQ/SQ)
correlation experiments. All these proton-detected pulse
sequences could provide atomic insights into the structure
and dynamics of organic and biological solids.
Poster 086
In situ Solid State Structural Studies of Anabaena
Sensory Rhodopsin in the E. coli Membrane
1
1, 2
3
Meaghan Ward ; Shenlin Wang ; Ivan Hung ; Peter L.
3
4
4
1
Gor'kov ; Yunjiang Jiang ; Hongjun Liang ; Leonid Brown ;
1
Vladimir Ladizhansky
1
2
University of Guelph, Guelph, Canada; Beijing NMR Center,
3
Peking University, Beijing, China; National High Magnetic
Field Laboratory, Tallahassee, FL;
4
Colorado School of Mines, Golden, CO
The membrane environment can affect the structure and
dynamics of membrane proteins. We demonstrate that solidstate NMR can be used to probe the structure of a seven
transmembrane helical photoreceptor, Anabaena sensory
rhodopsin (ASR), prepared in E.coli membranes. Due to the
excellent spectral resolution of peaks belonging to both ASR
and background proteins, and despite the small amount of
ASR in the NMR rotor, we are able to perform 3D experiments
and resolve ~40% of ASR residues in this environment.
Analysis of the NMR data indicates that the structure of ASR
is conserved, but subtly adapts to its environment. The high
Page 61
POSTERS
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
resolution of background peaks suggests that de novo
structural studies of these proteins may be possible.
Poster 087
DNP Enhanced Solid State NMR Observations in the L
and Mo Intermediates of Bacteriorhodopsin
1, 2
1, 2
1, 2
Qing Zhe Ni ; Eugenio Daviso ; Thach Can ; Marina
3
3
1, 2
Belenky ; Judith Herzfeld ; Robert Griffin
1
Department of Chemistry, Mass. Inst. of Tech., Cambridge,
2
MA; Francis Bitter Magnet Laboratory, Cambridge, MA;
3
Department of Chemistry, Brandeis University, Waltham, MA
Dynamic nuclear polarization has been utilized to enhance the
sensitivity of NMR signals by orders of magnitude. We present
an unprecedented enhancement of 400 on urea and 75 on
bacteriorhodopsin (bR) doped with AMUPol. One approach to
understand bR’s pump mechanism is by measuring the
changing distances between the Schiff base (SB) and active
site, such as Asp85 and Asp212. With DNP, their Cb-Cg cross
peaks can be seen for the first time in 2D RFDR –REDOR
filter experiments on L and Mo intermediates as well as on the
DA and LA resting states. Evidence of transfer of the SB
proton to D85 in Mo is seen by the shift in the D85bg cross
peak .
Poster 088
Multiple Acquisition of Magic Angle Spinning Solid-State
NMR Experiments Using One Receiver: Application to
Microcrystalline and Membrane Protein Preparations
Gopinath Tata; John Lee; Vitaly Vostrikov; Gianluigi Veglia
University of Minnesota, Minneapolis, MN
Magic angle spinning solid-state NMR (MAS ssNMR)
spectroscopy is emerging as a unique method for the atomic
resolution structure determination of biomacromolecules, such
as membrane proteins and fibrils that are recalcitrant to
crystallization. However, sensitivity and resolution of the
ssNMR spectra still limit the routine application of these
techniques, particularly for membrane proteins, where lipids
are used in the preparations to maintain the native conditions
of the proteins. In this work, we use DUMAS (dual acquisition
magic angle spinning) approach to build a library of new pulse
schemes that acquire multiple 2D and 3D spectra in a single
experiment using commercial ssNMR probes and single
receiver. Application of these methods on various membrane
proteins will be demonstrated.
Poster 089
The Effect of Ionic Liquids on
Protein Structure and Dynamics
1
1
2
Lisa Warner ; Erica Gjersing ; Sergei Dzyuba ;
3
Krisztina Varga
1
2
National Renewable Energy Lab, Golden, CO; Texas
Christian University, Fort Worth, TX;
3
University of Wyoming, Laramie, WY
Ionic liquids (ILs) are materials composed entirely of ions, with
solid-liquids phase transition at or below 100˚C. Despite the
complex nature of the solute-IL interactions, ILs are being
used as novel solvents for organo- and biocatalysis. Certain
ILs positively affect protein biochemistry, including enhanced
stability and enzymatic efficiency, others reportedly act as
denaturants. ILs can greatly increase efficiency of extracting
renewable energy products. However, the effect of ILs on the
enzymes that are integral to harvesting cellulose, lipids, and
sugars from renewable resources (e.g. plants/algae) must be
considered before inclusion in manufacturing. Generally, the
Page 62
interactions between ILs and proteins are not well understood.
We will present our NMR study of the effect of imidazoliumbased ILs on GB1 structure and dynamics.
Poster 090
Accurate NMR Determination of C-H/N-H Distances for
Unlabeled Molecules
1
2
2
Jean Paul Amoureux ; yusuke Nishyama ; Michal Malon ;
3
3
3
Marek Potrzebowski ; Piotr Paluch ; Tomasz Pawlak ; agata
3
4
6
Jeziorna ; Martin Dracinsky ; Julien Trébosc ;
5
Tatyana Polenova
1
Lille university and ECNU Shanghai, Villeneuve D'ascq,
2
3
France; RIKEN CLST-JEOL, Yokohama, Japon; Polish
4
Academy of Sciences, Lodz, Poland; Institute of Organic
Chemistry & Biochemistry, Prague, Czech Republic;
5
Department of Chemistry and Biochemistry, Newark, DE;
6
Lille university, Lille, France
CP-VC is very efficient at ultra-fast MAS to measure
accurately the dipolar interactions corresponding to H-C and
H-N short distances, which are very useful for resonance
assignment and for analysis of dynamics. Indirect H-C-H CPVC allows a gain of 6 in time. At ultra-fast MAS, only remain
along the indirect dimension a central and two positive peaks
separated by the dipolar interaction divided by 2. The widths
of these three peaks decrease with increasing speed, hence
leading to a better accuracy of the distance determination. As
long as only the dipolar peak separations are used, CP-VC is
very robust with respect to rf-inhomogeneity and to offsets.
Poster 091
T1 Relaxation-Compensated Difference Spin Diffusion
NMR and Aromatic Selection Techniques for Biological
Solid-State NMR
1
1
2
Jonathan Williams ; Tuo Wang ; Klaus Schmidt-Rohr ;
1
Mei Hong
1
Massachusetts Institute of Technology, Cambridge, MA;
2
Brandeis University, Waltham, MA
We introduce three techniques to simplify, resolve and assign
13
13
solid-state NMR 2D C- C correlation spectra. The first
technique involves the addition of a z-filter to the PDSD
13
experiment to compensate for C T1-relaxation, so that
difference spectra between two mixing times can be obtained
to exhibit only long-range correlation signals. The second
1
method uses gated H decoupling to suppress protonated
13
13
aromatic C signals while leaving only the quaternary C
signals, thus reducing aromatic region resonance overlap.
1
13
The third method utilizes chemical shift filters and H- C
recoupling to selectively detect Cα and Cβ resonances of
aromatic residues while suppressing aliphatic residue signals.
We demonstrate these methods on several model
compounds, including crystalline peptides and proteins,
membrane-bound peptides and plant cell walls.
Poster 092
SSNMR Studies of Membrane Curvature Induction by the
Influenza M2 Protein and Structure of a de novo Designed
2+ +
Zn /H Transporter
Tuo Wang; Mei Hong
Massachusetts Institute of Technology, Cambridge, MA
31
13
Novel P and C solid-state NMR experiments based on
oriented bicelles are used to determine membrane-curvature
induction by the influenza M2 peptide. An amphipathic helix in
M2 induces high curvature to the membrane, as revealed by
31
1
the P spectra. Indirectly detected H relaxation times and
POSTERS
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
31
1
off-magic-angle-spinning P- H correlation spectra indicate
that the majority of M2 binds the high-curvature membrane.
We also investigated a membrane transporter, ROCKER,
19
13
designed by DeGrado and coworkers, using F and C spin
diffusion NMR. The data show that ROCKER forms a
membrane-inserted antiparallel tetramer. Peptide dynamics
2+
and chemical shift perturbation by Zn binding indicate
peptide conformational changes, which give insight into the
ion transport mechanism.
Poster 093
Solid-State NMR Studies of the Conformation and Lipid
Interactions of a Viral Fusion Protein
1
1
2
3
Hongwei Yao ; Yu Yang ; Michelle Lee ; Alan Waring ;
2
1
Gerard Wong ; Mei Hong
1
Massachusetts Institute of Technology, Cambridge, MA;
2
University of California, Los Angeles, Los Angeles, CA;
3
University of California, Irvine, Irvine, CA
Using magic-angle-spinning solid-state NMR and small-angleX-ray scattering, we investigated the structure and lipid
interactions of the transmembrane domain (TMD) of a
parainfluenza virus fusion protein. The β-strand conformation
converts the phosphoethanolamine (PE) membrane to a
bicontinuous cubic phase, which is rich in negative Gaussian
31
P
curvature characteristic of hemifusion intermediates.
relaxation NMR data indicate that such cubic-phase
membranes can be distinguished from isotropic micelles by
their distinct T2 relaxation times. Interestingly, a chimera of
TMD and the fusion peptide (FP) is predominantly α-helical
but still causes an isotropic peak in PE membranes. These
structural features and FP-TMD interactions likely play an
important role in virus entry, by facilitating suitable membrane
topological changes.
Poster 094
Proton-Detected Solid-State NMR Spectroscopy of Bone
with Ultrafast Magic Angle Spinning
1
2
3
Kamal Mroue ; Yusuke Nishiyama ; Manoj Pandey ; Bo
1
1
1
1
Gong ; Erin McNerny ; David Kohn ; Michael Morris ;
1
Ayyalusamy Ramamoorthy
1
2
University of Michigan, Ann Arbor, MI; JEOL Ltd., Tokyo,
3
Japan; RIKEN CLST-JEOL Collaboration Center,
Yokohama, Japan
The inherent complex and heterogeneous structure of bone
poses significant challenges to traditional spectroscopic
techniques at fully understanding the the effects of aging and
diseases on bone. Recent advances in MAS NMR probe
technology have rendered 100-110 kHz spinning frequencies
1
feasible. Thus, H-detected NMR experiments that have
traditionally been challenging on rigid solids can now be
1
implemented. We have applied multidimensional H-detected
NMR measurements on bone under ultrafast MAS conditions.
1
1
Our investigations demonstrate that two-dimensional H/ H
chemical shift correlation spectra for bone can be obtained
using fp-RFDR (finite-pulse radio frequency-driven dipolar
recoupling) pulse sequence under 100 kHz MAS. Our results
1
1
infer that water exhibits distinct H− H dipolar coupling
networks with each of the backbone and side-chain regions in
collagen.
Poster 095
Structure and Topology of the M2 Proton Channel of the
Influenza A and B Viruses from Solid-State NMR
Jonathan Williams; Mei Hong
Massachusetts Institute of Technology,
Cambridge, MA
Using solid-state NMR heteronuclear correlation experiments,
we have measured water polarization transfer to the
transmembrane domain of the influenza AM2 protein to obtain
information on the structure of this tetrameric proton channel.
Despite various dependencies, the initial transfer rates reflect
the periodic nature of the residue positions from the waterfilled pore.
We also present initial solid-state NMR
characterization of the transmembrane domain of the
influenza BM2 proton channel, a functional analog of the AM2
channel.
Poster 096
Site-specific Structure and Dynamics of the Tubular
Assembly of Rous Sarcoma Virus Capsid Protein by
ssNMR and TEM
Jaekyun Jeon
University of Central Florida, Orlando, FL
Rous Sarcoma Virus (RSV) belongs to retroviral family and
shares many common features as its relative HIV. Its capsid
(CA) proteins self-assemble into pleomorphic polyhedral
shells encapsulating the viral genome. We prepared highly
uniform tubular assembly samples with RSV CA proteins that
exhibit sharp 6 fold symmetry under diffraction. High quality
spectra were obtained with such samples with average
linewidth for 13C 0.4 ppm and 15N 0.6 ppm. Selectively
labeled samples by 1,3- and 2-13C glycerol were produced to
assist the residue type assignments, in addition to two
samples with leucine and arginine uniformly 13C labeled.
Combined, we were able to sequentially assign 60% of the
protein and derived the secondary structures in assembled
state.
Poster 097
Solid-state NMR Studies of Peptidoglycan and Wall
Teichoic Acid in Staphylococcus aureus Whole Cells and
Isolated Cell Walls
Joseph Romaniuk; David Rice; Lynette Cegelski
Stanford University, Stanford, CA
The cell wall of Staphylococcus aureus is a thick insoluble
heterogeneous matrix that protects the bacterium against
external stresses, and is essential to cell viability. Thus, many
antibiotics target cell-wall synthesis. Measurements of cellwall architecture and composition are critical to examining cell
walls and antibiotic influences, and to developing new drug
treatment strategies. We use solid-state NMR to study cellwall composition and assembly in the context of intact
bacterial cells.
With CPMAS, REDOR, and DARR, we identify carbon,
nitrogen, and phosphorous pools unique to the cell wall in
uniformly-labeled whole-cell samples of S. aureus. These
strategies yield spectra that are information rich, and
signatures that are valuable in assessing the influence of
antibiotics on the organization of cellular systems.
Page 63
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
Poster 098
Structure Determination of the Drug Transporter EmrE
using MAS and Oriented Solid-State NMR Restraints
James Banigan; Maureen Leninger; Anindita Gayen;
Nate Traaseth
New York University, New York, NY
Multidrug efflux pumps are a primary mechanism in which
bacteria become resistant to drugs. In this study, we
reconstituted the multidrug transporter EmrE into lipid bilayers
to probe the drug-free structure using magic-angle-spinning
solid-state NMR spectroscopy as well as reconstituting it into
magnetically aligned bicelles to probe the helical geometries
with respect to the bilayer using oriented solid-state NMR
spectroscopy. The results outlined in this study give detailed
insight into how the small multidrug resistance protein family
binds and transports ligands.
Poster 099
Using Solid-State NMR to Define the Global Architecture
of Escherichia coli UTI89 Extracellular Matrix
Courtney Reichhardt; David Rice; Lynette Cegelski
Stanford University, Stanford, CA
Most microbes live as biofilms, which are communities of
microbes living in their secreted extracellular matrix (ECM).
Biofilms confer resistance to antibiotics and contribute to
serious and chronic infectious diseases. We previously
employed solid-state NMR to quantitatively determine that
uropathogenic E. coli UTI89 ECM is composed of two
biopolymers: the functional amyloid curli and cellulose. The
unique physical properties of ECM likely depend upon a
specific arrangement of its biopolymers. To elucidate the
structural arrangement and spatial dimensions of curli and
cellulose within the ECM, we have employed solid-state NMR
including spin-diffusion experiments such as DARR and
frequency-selective REDOR. Overall, we aim to a global
accounting of the interactions between the components of this
functional complex, multicomponent biopolymer blend.
Poster 100
15
Differentiation of Histidine Tautomeric States using N
13
Selectively Filtered C Solid-State NMR Spectroscopy
1
1
1
Riqiang Fu ; Yimin Miao ; Timothy A. Cross
1
National High Magnetic Field Laboratory, Tallahassee, FL
The histidine imidazole ring in proteins usually contains a
mixture of three possible tautomeric states (two neutral - t and
p states and a charged state) at physiological pHs. Here, we
15
13
demonstrate 1D N selectively filtered C solid-state NMR
spectroscopy to differentiate histidine tautomeric states and to
13
identify all C resonances of the individual imidazole rings in
15
a mixture of tautomeric states. When N selective 180°
pulses are applied to the protonated or non-protonated
13
nitrogen region, the C sites that are bonded to the nonprotonated or protonated nitrogen sites can be identified,
respectively. This proposed methodology opens up a new way
of differentiating the tautomeric states and investigating
histidine pH titration processes in functionally important
biological systems.
Poster 101
2
Using H Solid-State NMR to Probe Leucine Side Chain
Dynamics in an Amphiphilic Peptide upon Silica Coprecipitation
Helen Ferreira; Gary Drobny
University of Washington, Seattle, WA
Page 64
Biology uses a number of peptides to assemble silica
structures of controlled morphology. Biomimetic precipitation
studies have shown that LKα14, a synthetic amphiphilic
peptide, co-precipitates with silica to form nanospheres. In
solution, LKα14 aggregates into tetrameric bundles, which
could serve as a scaffolding for the silica co-precipitation. We
2
use deuterium solid state nuclear magnetic resonance ( H
ssNMR) to establish how the leucine side chain dynamics of
LKα14 differ in the neat state, buffered state, and silica
2
precipitated form. Modelling the H ssNMR lineshapes allows
us to probe the mechanism of peptide pre-aggregation and
silica co-precipitation.
Poster 102
Spatial Analysis of RF-Field inhomogeneity to Explain
Sequence Efficiency under MAS
1
1
2
Julien Trebosc ; Olivier Lafon ; Jean Paul Amoureux ; Piotr
3
3
Paluch ; Marek Potrzebowski
1
UCCS-CNRS UMR8181-Université de Lille, Villeneuve
2
D'ascq Cedex, France; Lille university and ECNU Shanghai,
3
Villeneuve D'ascq, France; Polish Academy of Sciences,
Lodz, Poland
Probes can present a large inhomogeneity of rf field across
the rotor volume which impair the analysis of experiments as
simple as a single pulse. We extend the analysis of rf-field
inhomogeneity (nutation experiment with fourier analysis) to
multiple dimension in CPMAS experiment. This allows us to
demonstrate the validity of CPVC approach to measure HC
distances under high spinning speed condition.
We describe a peculiar phenomenon of “rf-field spinning
sidebands” that can be explained by the modulation of B1 field
as the sample moves into different B1 zones during the
rotation.
We demonstrate the use of imaging the RF field using shim
gradient to evidence the migration of an adamantane sample
from the center to the extremities of a rotor.
Poster 103
Cellular Solid-State NMR Spectroscopy on Outer
Membrane Proteins from Corynebacteriales
1
1
1
Clement Carel ; Valerie Reat ; Marielle Tropis ; Mamadou
1
2
1
1
Daffe ; Roland Freudl ; Pascal Demange ; Alain Milon ;
1
Marie Renault
1
2
IPBS (UMRCNRS-UPS 5089), Toulouse, France; Institut für
Bio- und Geowissenschaften 1, Biotech, Jülich, Germany
Mycobacterium tuberculosis and other Corynebacteriales
possess a complex cell envelope that helps bacteria to resist
drug treatment and survive the immune response. In the cell
envelope reside α-ramified and β-hydroxylated long chain
fatty acids, called mycolic acids, and outer membrane proteins
that play crucial roles in bacterial physiology and
pathogenicity. The cellular environment may be critical for
mycomembrane protein’s structure and function but attempts
to acquire atom-scale information in native-like environments
thus far remain elusive. We here report on recent progress to
infer
structural
and
dynamical
parameters
of
Corynebacteriale’s OMPs in their native environment using
emerging cellular solid-state NMR protocols which involve
dedicated protein expression routes and multi-dimensional
solid-state experiments on cellular preparations of increasing
molecular complexity.
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
Poster 104
O Experimental and Theoretical NMR: Structural Insight
into Bound Water Molecules in Crystalline Amino Acids
1
1
1
Eric Keeler ; Vladimir K. Michaelis ; Ta-Chung Ong ;
3
2
3
Kimberley Craigen ; Susanne Penzel ; John Wren ;
3
1
Scott Kroeker ; Robert Griffin
1
2
Francis Bitter Magnet Lab and MIT, Cambridge, MA; ETH
3
Zürich, Zürich, Switzerland; University of Manitoba,
Winnipeg, Manitoba
The importance of water in biological systems is well known;
however, the structure of water bound in biological solids is
not well known. As of now there are no studies of the structure
17
of water using O NMR due to the inherent difficulties
17
associated with O NMR (i.e., spin I=5/2, low natural isotopic
abundance, low gyromagnetic ratio). We present, the use of
17
O to study the bound water
solid-state NMR on
environments in a series of amino acids and dipeptides. Using
multiple magnetic fields, non-spinning and MAS experiments,
we determined a fingerprint region for the chemical shift of
water bound in biological solids.
17
Poster 105
Biomedical Technology Resource Center for NMR
Molecular Imaging of Proteins
Chin H. Wu; Anna De Angelis; Sang Ho Park; Stanley Opella
UC San Diego, La Jolla, CA
The Biomedical Technology Resource Center for NMR
Molecular Imaging of Proteins is dedicated to the study of
biological systems in supra-molecular assemblies. Our
principal focus is the study of structure and function of
membrane proteins in environments that mimic native
conditions, and especially of G-protein coupled receptors
embedded in liquid-crystalline phospholipid bilayers. The
Center includes five high-field NMR spectrometers devoted to
solid-state NMR (500 MHz to 900 MHz), equipped with homebuilt and commercial probes for both static oriented and Magic
Angle Spinning experiments. Recent solid-state NMR
methods, applications and technological developments will be
presented, including applications of our new 900 MHz, 1.3
mm probe for fast-MAS. The BTRC is supported by the
National Institute of Biomedical Imaging and Bioengineering
(P41EB002031).
Poster 106
Spin-Locking and Cross-Polarization under Magic-Angle
Spinning of Uniformly Labeled Solids
Ivan Hung; Zhehong Gan
NHMFL, Tallahassee, FL
15
13
Spin-locking is important for cross-polarization and N- C
coherence transfer. We present a study of resonant
13
C homonuclear and proton
interferences from CSA,
heteronuclear dipolar couplings to spin-lock under magicangle spinning. Various sources and conditions of signal loss
are identified allowing the selection of optimal rf fields for ZQ
15
13
and DQ N- C CP transfer.
Poster 107
Identification of Cis and Trans Peptide Bonds in Peptides
and Proteins by Solid-State NMR Spectroscopy
Dwaipayan Mukhopadhyay; Christopher Jaroniec
The Ohio State University, Columbus, OH
We present a MAS solid-state NMR experiment that enables
the peptide bond configuration for non-proline sequences to
be readily identified in residue-specific manner in uniformly
13C,15N-labeled peptides and proteins. The experiment
correlates the amide 15N-1H dipolar coupling of residue i with
the 13CO chemical shift anisotropy of residue i-1, where both
tensorial interactions are re-introduced using R-type symmetry
sequences. The experiment is demonstrated for model trans
and cis dipeptides, glycylglycine and 2,5-diketopiperazine,
and two proteins including GB3 and Y145Stop prion protein
amyloid fibrils.
Poster 108
Solid-state NMR of Proteins above
100 kHz Magic Angle Spinning
1
1
1
Loren B. Andreas ; Andrea Bertarello ; Diane Cala ; Daniela
1
1
1
2
Lalli ; Tanguy Le Marchand ; Jan Stanek ; Benno Knot ;
2
2
2
3
David Osen ; Alex Krahn ; Armin Purea ; Nicholas Dixon ;
2
2
1, 4
Sebastian Wegner ; Frank Engelke ; Lyndon Emsley ;
1
Guido Pintacuda
1
2
CNRS - ENS Lyon, Lyon, France; Bruker Biospin,
3
Rheinstetten, Germany; University of Wollongong,
4
Wollongong, Australia; EPFL, Lausanne, Switzerland
We describe here our first experiments on the GHz
spectrometer with a new Bruker MAS probe capable of
spinning samples at above 100 kHz in a 0.7mm rotor.
This new probe allows the efficient acquisition of tripleresonance spectra using less than 0.5 mg of deuterated
microcrystalline
proteins. We
observed
significantly
1
15
13
lengthened H, N and C lifetimes, allowing the design of
improved schemes for rapid unambiguous sequential
assignment. Finally, the new spinning regime halves the
1
homogeneous contribution to the H line-widths in fullyprotonated protein samples, increasing the impact of solidstate NMR to samples that cannot easily be deuterated.
Poster 109
13
15
A Band-selected C, N Solid-state NMR Experiment for
Characterization of Bacterial Cell Surfaces and
Extracellular Matrix
David M. Rice; Courtney Reichhardt; Joe Anthony Romaniuk;
Lynette Cegelski
Stanford University, Stanford, CA
13
15
Soild-state methods, using isotopic labels, such as C- N
13
13
REDOR or C- C DARR are important tools for identification
of the components and structure of bacterial cell surfaces and
13
extracellular matrix. We often uniformly enrich with C and
15
N and have introduced a band-selective REDOR experiment
13
combined with C DARR to identify resonances through
NCCN correlation. We use this experiment, for example, to
study the association of cellulose and amyloid protein in
extracellular matrix. Most often a band-selective 1D
experiment is preferable to 2D and we use larger, lowerspeed MAS rotors to improve sensitivity and stability. This
poster will describe the method and experimental issues such
as sideband-control that are associated with performing
robust band-selective NMR spectroscopy of cell surfaces.
Poster 110
Solid-State NMR Studies of Fibril Conformation and
Strain Diversity of Y145Stop Prion Protein Amyloids
1
1
1
Theint Theint ; Philippe S. Nadaud ; Jonathan J. Helmus ;
2
2
Krystyna Surewicz ; Witold Surewicz ; Christopher P.
1
Jaroniec
1
2
The Ohio State University, Columbus, OH; Case Western
Reserve University, Cleveland, OH
Page 65
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
We present the solid-state NMR study of mammalian prion
amyloids formed by Y145Stop prion variants including human,
mouse, and Syrian hamster, as well as several speciesmimicking mutants at critical amino acid residues. We have
identified single amino acids in the human protein sequence,
which allow it to mimic the conformation of another species
(112 for mouse and 139 for Syrian hamster). Our data also
provide insights into the observed differences in fibril
morphologies and cross-seeding specificities among the
mammalian prion variants.
Poster 111
Membrane Insertion Depth and Curvature Sensing
1
1
2
Erin Tyndall ; Richard Gill Jr. ; Kumaran Ramamurthi ;
1
Fang Tian
1
2
Penn State College of Medicine, Hershey, PA; National
Cancer Institute, Bethesda, MD
We will present a HRMAS study of the dependence of
membrane insertion depth on membrane curvature.
Membrane curvature is modeled with spherical nanoparticle
supported lipid bilayers. Our data support a hypothesis that
membrane curvature sensing is critically dependent on
membrane insertion depth.
Poster 112
Supramolecular Structure of a Peptide Amphiphile
Nanofiber Probed by Solid-State NMR Spectroscopy
1
2
1
Zhe Qi ; Charles Schwieters ; Christopher P. Jaroniec
1
2
The Ohio State University, Columbus, OH; National
Institutes of Health, Bethesda, MD
Solid-state NMR spectroscopy coupled with TEM, AFM and
XRD was used to study the supramolecular structure of
nanofibers assembled from the peptide amphiphile (PA),
palmitoyl-Val-Val-Ala-Ala-Glu-Glu-NH2. The -VVAA- portion
was found to adopt a parallel, in-register β-sheet structure
with an interstrand distance of ~4.8 Å. The palmitoyl tail is
incorporated into a densely packed fiber core and does not
undergo isotropic like motions. These structural restraints
were used to construct initial molecular models of the
nanofiber that are consistent with the experimental data.
Poster 113
Multiple Acquisitions and Correlation Spectroscopy for
13C and 1H detection in MAS
Bibhuti Das; Stanley Opella
UCSD, San Diego, CA
Solid state NMR study of biomolecules such as membrane
proteins in phospholipid bilayers are highly demanding and
require optimization of isotope labeling and pulse sequence
development to obtain high sensitivity and resolution data.
Here, we present new pulse schemes utilizing multiple
acquisitions and coherence transfer pathways to correlate
inter and intra residues in multi-dimensional experiments
recorded in a single shot. Magic angle spinning (MAS)
experiments optimized for 13C and 1H detection and
reduction in NMR measurement time, up to six fold,
incorporating non-uniform sampling schemes for multiple
acquisitions and correlation spectroscopy (MACSY) will be
discussed. Phase sensitive dipolar recoupling under magic
angle spinning along with the simultaneous acquisition of 1H13C and 1H-15N will be discussed.
Page 66
Poster 114
Interface Structure in HIV-1 Capsid Assemblies
Characterized by MAS NMR Spectroscopy and DNP
Marvin Bayro; Wai-Ming Yau; Kent Thurber; Robert Tycko
National Institutes of Health, Bethesda, MD
The 231-residue capsid (CA) protein of HIV-1 spontaneously
self-assembles into tubes with a hexagonal lattice that is
believed to mimic the surface lattice of conical capsid cores
within intact virions. We report the results of MAS NMR
measurements on HIV-1 CA tubes that provide new
information regarding changes in molecular structure that
accompany CA self-assembly, local dynamics within CA
tubes, and possible mechanisms for the generation of lattice
curvature. Further measurements targeted at the
intermolecular dimerization region is allowing us to refine the
structure of this important interface in the tubular lattice.
Among these measurements, sensitivity enhancement via
dynamic nuclear polarization at 25 K has permitted the
identification of intermolecular interactions in both assembled
samples and frozen protein dimer solutions.
Poster 115
NMR Studies of a GPCR Reconstituted in Phospholipid
Bilayers with Ligand Bound: CXCR1 and Interleukin-8
Sabrina Berkamp; Sang Ho Park; Bibhuti Das; Anna De
Angelis; Jasmina Radoicic; Mitchell Zhao; Stanley Opella
University of California, San Diego, La Jolla, CA
G-protein coupled receptors (GPCRs) are the largest family of
transmembrane receptors in eukaryotes and are associated
with many diseases. CXCR1 is a chemokine GPCR that has
one high-affinity ligand, Interleukin-8 (IL-8). We have
published the structure of CXCR1 as solved by MAS solid
state NMR spectroscopy previously. However, little atomicresolution data is available on a ligand-receptor complex. We
have used solid state NMR spectroscopy to study the IL-8 –
CXCR1 complex reconstituted in liposomes. Preliminary data
shows that CXCR1 undergoes a conformational change and
well as changes in dynamics in the ligand-binding site on the
flexible N-terminus. Additionally, fast (60 kHz) MAS protondetected experiments have enabled us to study IL-8
immobilized on the receptor and progress will be presented.
Poster 116
Oligomeric Structure of a Lipid-Reconstituted Membrane
Protein Determined by Double Electron-Electron
Resonance Spectroscopy
1
3
2
Sergey Milikisiyants ; Shenlin Wang ; Rachel Munro ;
1
2
1
Matthew Donohue ; Leonid Brown ; Tatyana Smirnova ;
2
1
Vladimir Ladizhansky ; Alex I. Smirnov
1
2
North Carolina State University, Raleigh, NC; University of
3
Guelph, Guelph, Ontario; Beijing Nuclear Magnetic
Resonance Center, Beijing, China
Oligomeric states of membrane proteins are commonly
observed in nature and may depend on the membranemimetic environment. Here, we demonstrate that Double
Electron-Electron Resonance (DEER) technique and direct
modeling
of
multispin
effects
provide
long-range
intermolecular distance restraints and allow for determination
of the oligomeric order without knowing exact efficiency of
spin-labeling. We combine DEER and NMR restraints
obtained in the lipid environment to show that the addition of
long-range electron distances refines structure of Anabaena
Sensory Rhodopsin.
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
Poster 117
Magic Angle Spinning NMR Characterization of Human
Dialysis-Related Amyloidosis (DRA) Fibrils
1
1
2
Yongchao Su ; Robert Silvers ; Clare L. Pashley ; Claire J.
2
1
1
Sarell ; Matthew Eddy ; Galia Debelouchina ; Sheena
2
1
Radford ; Robert Griffin
1
2
MIT, Cambridge, MA; University of Leeds, Leeds, UK
Pathological fibrils are associated with human amyloid
diseases. We utilize isotopic labeling strategies and multidimensional MAS NMR techniques to study dialysis-related
amyloidosis (DRA) fibrils, including β2m and its truncation
variant ΔN6. Interestingly, ΔN6 has been found to catalyze
β2m assembly at neutral pH. Similar fibril core have been
determined from nearly complete backbone assignment of the
13
15
two fibrils. Intermolecular C- N correlation experiments
have identified the parallel-in-register packing of ΔN6,
providing a representative case of the parallel packing of
pathological fibrils formed from antiparallel monomer at
physiological pH. Preliminary structural investigations of the
β2m/ΔN6 mixed fibrils suggest structural and dynamic
perturbation compared with their homofibrils, providing so far
the first study of copolymerized fibrils that are associated with
human fibril diseases.
DYNAMICS
118 - 142
Poster 118
The Dark Energy of Proteins Comes to Light: Motion and
the Creation of an NMR-based “Entropy Meter”
Vignesh Kasinath; Kyle Harpole; Jackwee Lim; Kathleen
Valentine; Veronica Moorman; Kendra Frederick;
Kim Sharp; Joshua Wand
Univ of Pennsylvania, Philadelphia, PA
Conformational entropy is a potentially important parameter
contributing to protein function. Quantitative measures of
conformational entropy are necessary for an understanding of
its role but have been difficult to obtain. We introduce an
empirical method that utilizes changes in conformational
dynamics measured by NMR relaxation as a proxy for
changes in conformational entropy. Molecular dynamics
simulations of seven proteins validate the use of
experimentally accessible measures of methyl motion - the
NMR-derived generalized order parameters - as a proxy from
which to derive changes in protein conformational entropy.
Experimental results from three dozen protein-ligand
complexes that indicate that the approach is general and that
the binding conformational entropy is often large. Supported
by the NIH and the Mathers Foundation.
Poster 119
Molecular Dynamics in a Glass-Forming Liquid using
Variable Temperature 2D PASS NMR Spectroscopy
1
2
1
Derrick Kaseman ; Bruce Aitken ; Sabyasachi Sen
1
University of California, Davis, CA;
2
Corning Inc., Corning, NY
The temperature dependence of the rotational dynamics of
P4Se3 molecules associated with shear relaxation of a glass31
forming liquid is studied using solid-state P 2D Phase
Adjusted Spinning Sideband (PASS) NMR spectroscopy.
Application of high-temperature PASS enables the separation
and observation of dynamical averaging of overlapping
31
chemical shift anisotropy tensors of multiple P sites provides
direct evidence supporting two types of molecular motion
occurring in different temperature regimes. In the low
temperature regime the molecules display characteristics of a
dynamically constrained liquid and perform uniaxial rotation
without significant translational diffusion. Further increase in
temperature results in a dynamical transition into isotropic
rotational reorientation expected in a regular liquid.
Poster 120
Cse4
,
Implication of Folding of Centromeric Protein CENP-A
and Its Interaction with Other Components, in the
Formation of Specialized Nucleosome
Nikita Malik; Sarath Chandra Dantu; Santanu Ghosh;
Ashutosh Kumar
Indian Institute of Technology Bombay, Mumbai, India
Cse4
, replaces Histone-3 in the
Centromeric protein, CENP-A
specialized nucleosome in eukaryotic cells. A discrepancy in
the formation of this structure causes chromosome
missegregation and thereby birth-defects and cancer. Our
study focuses on the structure and recognition dynamics of
Cse4
and its interaction with centromeric components.
CENP-A
We have initiated NMR studies on the unfolded protein,
wherein >90% of the 229 residues have been assigned; and
are tracing the residues which are involved in initial folding
steps, using NMR and biophysical techniques in conjunction
with MD. Our initial results suggest that the N- and C-terminus
fold independently and in absence of any interacting partner
the N-terminus may self interact, giving a clear indication of its
role in regulation of nucleosome formation.
Poster 121
Hyperpolarized Xenon-129 Relaxometry for
Chemical Sensing
Muller Gomes; Phuong Dao; Clancy Slack; Christophoros
Vassiliou; Ashley Truxal; Keunhong Jeong; David Wemmer;
Matt Francis; Alex Pines
University of California, Berkeley, Berkeley, CA
We report a new relaxation based xenon molecular sensor.
Unlike chemical shift or saturation transfer, this technique
does not require a strong external magnetic field. Xenon
relaxometry is extremely sensitive to binding events and to
different metal ions, with changes in relaxation approaching
one hundred percent for binding. These changes arise from
the change in rotational correlation time upon binding and
from the paramagnetism of the metal ions.
Poster 122
Dynamics of Guest Molecules in Metal-Organic
Frameworks (MOFs) Studied by 2H and 13C Solid-State
NMR
1, 2
2, 3
2
2
Haiyan Mao ; Farhana Gul-E-Noor ; Jun Xu ; Wei Wang ;
2
Yining Huang
1
2
Nanjing Forestry University, Nanjing, China; Western
University, London, Ontario;
3
Brooklyn College/CUNY, Brooklyn, NY
Porous coordination polymers (PCPs) or metal-organic
frameworks (MOFs) are hybrid inorganic-organic compounds
with 3-D structure and high surface area. In the present work
we report on study of guest dynamics in MOF MIL-53(Al) and
CPO-27-M (M=Ni and Co) MOFs. For this purpose, different
13
relative amounts of deuterated acetone [(CD3) 2CO] and CO2
were adsorbed with respect to metal atom in MIL-53(Al) and
CPO-27-M (M=Ni and Co), respectively. Variable temperature
2
13
H and C NMR spectroscopy is employed to follow the
dynamic features of guest molecules. From the analyses of
Page 67
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
observed characteristic
information is obtained.
lineshape
detailed
motional
Poster 123
Correlation of Backbone Dynamics with Pathogenic
Propensity of Transthyretin in Amyloidosis
Jitendra K. Das; Shyam S. Mall; Aritra Bej; Sujoy Mukherjee
CSIR - Indian Institute of Chemical Biology, Kolkata, India
Conformational excursions modulate the formation of nonnative intermediates leading to pathogenic conditions
involving protein aggregation. Most of the biophysical
techniques fail to characterize these poorly populated
transient intermediates. In our recent work (Das et al., Angew.
Chem. Int. Ed., 2014) we probed the backbone dynamics of
transthyretin (TTR) over an extended timescale by using NMR
spectroscopy and MD simulations. The backbone flexibility of
TTR causes its dissociation and destabilization leading to
fibrillization, as suggested by the location and extent of
backbone motions. Interestingly, population of intermediate
states increases from ~10% for wild type to ~28% for
pathogenic TTR mutants, which are energetically more
favorable than the wild type. These findings open a new
perspective of intermediates in TTR amyloidosis.
which act as proxies for peptide planes and sidechains,
respectively. We present both a structure-free analysis and
ensemble calculations to derive a dynamic correlation map for
GB3.
Poster 126
Protonation of a Glutamate Residue Modulates the
Exchange Dynamics and Resting Conformation of the
Drug Transporter EmrE
Maureen Leninger; Anindita Gayen; Nate Traaseth
New York University, New York, NY
Secondary active transporters provide one of the
primary mechanisms of multidrug resistance in bacteria
through the transport of lethal drugs across the membrane
and out of the cytoplasm. Antiporters from the small multidrug
resistance (SMR) family represent an excellent system to
study ion-coupled transport due to their small size and
importance in antiseptic resistance. EmrE is the model SMR
protein and carries out drug efflux by coupling with the
electrochemical potential across the inner membrane of E.
coli. In this work, we used solution and solid-state NMR
spectroscopy to elucidate the molecular basis for active
transport within the SMR family where the resting
conformation and dynamics of the protein are regulated by the
protonation state of a conserved glutamate residue.
Poster 124
High-Resolution Conformation and Dynamics of Human
VDAC1 in a Solution Environment
1
1, 2
1
Mariusz Jaremko ; Lukasz Jaremko ; Saskia Villinger ;
1
1
1
Christian Schmidt ; Christian Griesinger ; Stefan Becker ;
1, 2
Markus Zweckstetter
1
Max-Planck-Institut für Biophysikalische Chemie, Goettingen,
2
Germany; Deutsches Zentrum für Neurodegenerative
Erkrankung, Goettingen, Germany
NMR spectroscopy provides access to dynamics of
membrane proteins in solution, but it is often a challenge to
obtain sufficient structural information. Very powerful and so
far the most accurate long range structural information is
obtained through residual dipolar couplings, but recording
high-quality spectral data for membrane proteins in the
environment of an alignment medium is often impossible.
Here we show that 15N R1 and R2 relaxation rates enable the
structure refinement and dynamics analysis of membrane
proteins. We managed to refine the NOE-based 3D structure
of the E73V mutant of hVDAC1 with spin relaxation rates from
three fields. Analysis of the 15N relaxation data sets revealed
complex backbone dynamics.
Poster 127
3
Concerted Analysis of J Couplings for Quantitative
Assessment of Protein Backbone Dihedral Angle
Dynamics
Jung Ho Lee; Fang Li; Alexander Grishaev;
Jinfa Ying; Ad Bax
National Institutes of Health, Bethesda, MD
3
J couplings are related to backbone dihedral angles of
proteins by Karplus equations. Here, we show that concerted
3
analysis of J couplings can provide new information on
3
3
dynamic angular distributions of ϕ. Analysis of JHNHα and JC'C'
couplings can provide quantitative information on ϕ and its
amplitudes of motion, σ. The σ values are compared to the
results from NMR-derived ensembles and MD simulation. We
expect that the current approach will provide an alternative
way of measuring amplitudes of motion and refining backbone
angle distributions, especially for highly dynamic and
intrinsically disordered proteins. Analysis of α-synuclein
reveals that the protein has rather homogeneous σ values of
29±3º.
Poster 125
Direct Detection of Slow Correlated Dynamics in Proteins
via Dipolar Interactions
1
2
Beat Vogeli ; R. Bryn Fenwick
1
Swiss Federal Institute of Technology, ETH Zurich, Zürich,
2
Switzerland; The Scripps Research Institute, La Jolla, CA
It has been a long-standing challenge to detect concerted
protein motion, as its understanding would offer valuable
insight into entropy contributions, catalysis, allostery, etc. The
methods proposed so far rely on an indirect way of
identification: Typically, observables are used to calculate
structural ensembles, which in turn exhibit correlations. One
such observable per se, however, does not contain such
information. Here we propose a strategy for direct observation
of correlated motion that relates cross-correlated relaxation
(CCR) rates between dipolar interactions to residual dipolar
couplings of individual consecutive HN–N and Hα–Cα bonds,
Poster 128
NMR Relaxation and Diffusion Studies of Bone Water
1
2, 4
Farhana Gul-E-Noor ; Chandan Singh ; Antonios
3
2
1, 3
Papaioannou ; Neeraj Sinha ; Gregory Boutis
1
2
Brooklyn College/CUNY, Brooklyn, NY; Center of
3
Biomedical Research, Lucknow, India; Graduate Center of
4
The City University of New York, New York, NY; School of
Biotechnology, Varanasi , India
We report on an experimental study of water dynamics in
2
cortical bone by deuterium ( H) T1-T2, T2-T2 and D-T2 NMR
methodologies. By systematic exposure of the bone to EDTA
(ethylenediaminetetraacetic acid) or collagenase we were
able to assign the various peaks observed in the 2D T1-T2
relaxation maps. T1-T2 studies in fractured bone, bone under
applied force and mechanical wear were carried and provide
additional insight into architectural changes that influence the
dynamics and populations of various water reservoirs.
Page 68
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
Diffusion-T2 experiments were also performed and the
diffusion coefficients of different water reservoirs were
13
measured. Additionally, C CP MAS NMR (cross-polarization
under magic angle spinning) experiments on collagenase and
EDTA treated samples were performed to verify the treatment.
Poster 129
Mapping the Hierarchical Protein Conformational Energy
Landscape using Temperature-Dependent Multinuclear
Spin Relaxation Measurements
2
4
3
Jozef Lewandowski ; Meghan Halse ; Lyndon Emsley ;
1
Martin Blackledge
1
2
Institut de Biologie Structurale, Grenoble, France; University
3
of Warwick, Coventry, UK; ENS Lyon, Villeurbanne, France;
4
University of York, York, UK
Understanding the hierarchy of the protein conformational
energy landscape holds the key to deciphering how proteins
function at physiological temperatures. Here we use
multinuclear NMR relaxation measurements in a hydrated
nanocrystalline protein to examine the hierarchy of protein
dynamics occurring at temperatures from 105 to 280 K.
Thirteen relaxation rates are used to probe the evolution of
dynamic modes and timescales in both protein and solvent,
providing the basis for a coherent interpretation of the
interplay between different modes that are observed for the
individual components of this complex system. The results
support strong coupling between protein and solvent
dynamics above 160 K, with fast motions in solvent, then slow
side chain motion, then fast backbone motions being activated
consecutively.
Poster 130
Interactions and Dynamics of the Disordered C-terminal
Domain of Artemis
1
2
1
Cyril Charlier ; Ludovic Carlier ; Philippe Pelupessy ; Ching1
3
4
Yu Chou ; Dimitrios Sakellariou ; Geoffrey Bodenhausen ;
5
5
1
Patricia Cortes ; Aneel K. Aggarwal ; Fabien Ferrage
1
2
CNRS - ENS, Paris, France; UPMC Université Paris 06,
3
4
Paris, France; CEA Saclay, Gif-Sur-Yvette, France; EPFL
5
SB ISIC LRMB, Lausanne, N/A; Icahn School of Medicine at
Mount Sinai, New York, NY
Artemis, an endonuclease and exonuclease that plays a
crucial role in the immune adaptive system contains a long
disordered C-terminal region (310 residues). Here, we used
NMR to study Artemis and its complex with Ligase IV. We
assigned backbone resonances of a 104-residue fully
disordered construct of Artemis, which includes the binding
15
site to Ligase IV. Combining NMR-based titration and N
CPMG dispersion, we characterized the dynamics of the
binding event and identified a five-residue extension of the
binding region. We also carried out extensive relaxation
measurements at several magnetic fields using conventional
methods and R1 measurements at low magnetic field with
high-resolution relaxometry to access to the distribution of psns motions in Artemis.
Poster 131
Dynamics and Chemical Exchange Studies on Human
Eye Lens γS-crystallins
1
1
1
Suvrajit Sengupta ; Natalia Kozlyuk ; Domarin Khago ;
1
2
Carolyn N. Kingsley ; William D. Brubaker ;
1, 2
Rachel W. Martin
1
Department of Chemistry, University of California, Irvine, CA;
2
MB & B, University of California, Irvine, CA
The γS-crystallin protein is the most abundant structural
protein in the human eye lens cortex. Its G18V variant is
involved in childhood-onset cortical cataract. In previous work
(Kingsley et al., Structure, 21, 2221, 2013), we have shown
that the G18V variant remains folded and retains the two
double Greek key domains characteristic of the wild type (WT)
variant. In this work, we characterize the backbone dynamics
in WT and G18V γS-crystallins in a site specific manner using
15
15
15
N R1 and R2 relaxation experiments, and N- N nuclear
2
Overhauser enhancement experiments. In addition, H
exchange experiments were carried out to monitor solvent
accessibility and large amplitude motions.
Poster 132
Insights into Nucleotide Binding of DNA Polymerase β
Using NMR Spectroscopy
Beth Moscato; J. Patrick Loria
Yale University, New Haven, CT
DNA Polymerase β (Pol β) plays a crucial role in the DNA
repair pathway; point mutations have been linked to cancer.
Here, we use TROSY-optimized 1H-15N HSQC techniques to
characterize the structure and dynamics of both wild-type
(WT) and mutagenic point mutant I260Q Pol β through the
DNA repair process. In both free enzymes, dispersive
behavior is observed in residues associated with DNA
binding; addition of gapped DNA quenches these motions.
DNA-bound I260Q Pol β exhibits more conformational
flexibility than the WT complex; line shape analysis of
behavior upon titration of the binary complexes with
nucleotide is in best agreement with a model in which domain
closure upon nucleotide binding is both slower and less
energetically favorable in the mutant.
Poster 133
Dynamics in Nuclear Spin Chains Coupled to a
Controllable Environment
Xuan Wei; Ashok Ajoy; Gurneet Kaur; Paola Cappellaro
MIT, Cambridge, MA
We explore experimentally the nuclear spin dynamics in
quasi-one-dimensional chains in crystal of fluorapatite, while
retaining interactions to the chain environment. We observe
an increase in oscillation frequency of the total magnetization
and multiple quantum coherences (MQC). The observed
dynamics due to the spin environment can be modeled by the
presence of a uniform magnetic field, thus enabling simple
control sequence to decouple it from the spin chain system.
Poster 134
RNA Binding Alters the Backbone Dynamics of SNF RNA
Recognition Motif
Kathleen Hall; Greg DeKoster
Washington Univ Med Sch, Saint Louis, MO
The SNF RNA Recognition Motif (RRM) is an 11 kDa α/β
sandwich protein domain that uses its β-sheet to bind the
RNA loop of either of two RNA hairpins. SNF RRM alone has
-1
extensive slower backbone dynamics (ΔR2 = 10-40 sec )
throughout the body of the domain, especially prominent in
one α-helix and one loop. When one RNA is bound, SNF's
backbone dynamics change; most slower motions disappear,
and those remaining are restricted to the helix and loop. Here
we compare the dynamics of SNF to those of U1A RRM when
both are bound to the same RNA, to elucidate their different
binding mechanisms.
Page 69
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
Poster 135
Backbone Dynamics of Antifreeze-Like Domains of Sialic
Acid Synthase and Its Mutant are Compared Type III
Antifreeze Proteins
Seo-Ree Choi; Joon-Hwa Lee
Gyeongsang National University, Jinju, South Korea
Sialic acids play a vital role in a variety of biological functions
and are synthesized by sialic acid synthase (SAS). SAS
consists of an N-terminal catalytic domain and a C-terminal
antifreeze-like (AFL) domain. The AFL domain of the N.
meningitides SAS (nmAFL) and human SAS (hAFL)
contributed to the substrate binding of SAS. The type III
antifreeze proteins (AFPs) are found in a variety of coldadapted organisms to promote survival at subzero
temperatures and consist of one α-helix, three 310-helices,
and two β-strands.
In this study, we have investigated backbone dynamics of
hAFL and nmAFL as well as the type III AFP (HPLC12
isoform). This study provides insight intomolecular basis for
the different biological working temperatures of these
homologous proteins.
Poster 136
Dynamics of Hydrophobic Core in Amyloid Fibrils
Investigated at Methyl Sites Using
2
H Static Solid-state NMR
1
1
2
Liliya Vugmeyster ; Matthew A. Clark ; Gina Hoatson ;
3
Robert Tycko
1
2
University of Alaska Anchorage, Anchorage, AK; College of
3
William and Mary, Williamsburg, VA; National Institutes of
Health, Bethesda, MD
We present preliminary results on studies of hydrophobic core
dynamics of amyloid fibrils comprised of native Aβ1-40 protein.
Static deuterium NMR line shape measurements in samples
with selectively labeled methyl groups indicate presence of
extensive ms-µs time scale dynamics, which linger down to
about 200-180 K. We also probe the dynamics in two
different morphological states of the fibrils, which differ in their
levels of cytotoxicity.
Poster 137
NMR Structural and Dynamics Studies of New Insulin
Analog Comparing with Human Insulin
Wojciech Bocian; Elzbieta Bednarek; Jerzy Sitkowski;
Lech Kozerski
National Medicines Institute, Warsaw, Poland
The insulin is a polypeptide hormone which regulates the
metabolism of carbohydrates and fats by promoting the
absorption of glucose from the blood. It is postulated that
formation of insulin-receptor complex is associated with broad
conformational changes in the peptide. Here we present the
comparison of structure and dynamics of human (HI) and
engineered insulin (SK3R). The dynamic of insulin chains was
examined by 15N relaxation measurements and model-free
approach. Deuterium exchange measurements were done
using time-resolved non uniform sampling methodology. The
results from NMR experiments were compared with molecular
dynamics calculations. The C-termini B-chain of SK3R insulin
analog exhibit significantly increased dynamics. This probably
can partly explain the observed differences in the biochemical
properties of both insulins.
Page 70
Poster 138
Fast Field Cycling NMR Relaxometry: From Molecular
Dynamics to Practical Applications
Gianni Ferrante
Stelar s.r.l., Mede (Pv), Italy
Molecular dynamics are critical to understanding intra- and
inter-molecular events affecting molecular interactions in
condensed phases. One of the most efficient means for
characterizing molecular dynamics at long time scales is
magnetic spin relaxation. In particular, the magnetic field
dependence of the nuclear spin-lattice relaxation rate
constant, 1/T1 provides a direct measurement of the spectral
density functions that characterize molecular motions.
Fast Field Cycling (FFC) NMR relaxometry is used to
measure the spin-lattice relaxation dispersion profile efficiently
over nearly five decades in Larmor frequency from 10 kHz to
42 MHz and higher in a fully automated mode.
Herein we discuss several key applications of the technique
and how these may be important in solving some practical
research and industrial problems.
Poster 139
Pico- to Nanosecond Motion in Protein Sidechains
Explored with a Combination of High-Field Relaxation and
High-Resolution Relaxometry
1
1
2
Samuel Cousin ; Cyril Charlier ; Thorsten Marquardsen ;
3
1
Geoffrey Bodenhausen ; Fabien Ferrage
1
2
CNRS - ENS, Paris, France; Bruker BioSpin, Rheinstetten,
3
Germany; EPFL SB ISIC LRMB, Lausanne, Switzerland
Understanding protein dynamics at atomic resolution is
necessary to describe bio-chemical processes that compose
living cells at atomic resolution. An objective of our work is the
full characterization of the spectral density function for a set of
probes of protein motions.
We use a shuttle device developed by Bruker Biospin to
measure relaxation at low magnetic fields with the resolution
of a 600 MHz spectrometer. Using this high-resolution
relaxometry approach, side chain motions have been
evaluated in a model protein (Ubiquitin) using methyl group of
13 2
1
isoleucine { C H2 H}. Carbon-13 longitudinal relaxation rates
were measured over a broad range of magnetic fields and
complemented by precise high-field relaxation rates.
Poster 140
Investigating Chemical Exchange in Albumin Solution
through Multiexponential Transverse Relaxation
Dispersion Analysis
Ping-Chang Lin
Howard University, Washington, DC
Conventional NMR methods are inapplicable to investigating
chemical exchange in a complex system. Here, we propose a
procedure integrating <g class="gr_ gr_7 gr-alert gr_spell
ContextualSpelling" id="7" data-gr-id="7">nonnegative</g>
least squares (NNLS) analysis of multiexponential T2
relaxation into transverse relaxation dispersion experiment to
probe chemical exchange in a complex system. The approach
19
was validated via F T2 relaxation data of 6-fluoro-DLtryptophan in a two-compartment system with and without
bovine serum albumin. The nature of two distinct T2 peaks in
the NNLS-analyzed T2 distribution indicated 6-fluoro-DLtryptophan either in the free state or in interconversion while
the sample quantity was reflected by quantitating the
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
associated T2 peak areas. Further, the relaxation dispersion
analysis estimated the exchange rate and dissociation
constant between the free and albumin-bound states in the
fluorinated tryptophan-albumin solution.
Poster 141
Dissection of the Water Cavity of Yeast Thioredoxin
1
1
1
Mariana de Magalhães ; Adolfo Moraes ; Anwar Iqbal ;
2
1
1
Francisco Gomes-Neto ; Ana Paula Valente ; Fabio Almeida
1
Federal University of Rio de Janeiro, Rio De Janeiro, Brazil;
2
Oswaldo Cruz Institute, Rio de Janeiro, Brazil
The water cavity of yTrx1 is ancestral, conserved and poorly
understood. It shows complex dynamics, responsible for
catalytic-relevant events, coupling hydration, water exchange,
and loop motions. Studies of molecular dynamics enabled a
detailed description of the water cavity. It connects the
interacting loops, β-sheet and α-helices 2/4. It has 3 lobes: A,
B and C. Lobe A is hydrophilic and superficial. Lobe B is the
central formed by the catalytic Cys33/Asp24. Lobe C is
hydrophobic and conserved cis-Pro73. We performed 1HN
and 15N CPMG and R1rho relaxation dispersion to
understand the dynamics of the cavity. The results indicate
independent fast exchange motions, revealing that
independent forces other than solvation of Asp24 maintain
lobe A and C in the open configuration.
Poster 142
TROSY Pulse Sequence for Simultaneous Measurement
of Relaxation Rates in Deuterated Proteins
Paul O'brien; Arthur G Palmer
Columbia University, New York, NY
We present a novel TROSY pulse sequence for measurement
15
of both the N longitudinal relaxation rate constant R1 and
15
1
dipolar cross-relaxation rate between N and H nuclei.
15
Accurate quantification of the N R1 rate and steady-state
15
1
N-{ H} NOE is vital for understanding fast dynamic
processes along the protein backbone. By utilizing
1
unperturbed H magnetization, our pulse sequence allows
measurement of the Boltzmann NOE intensity followed by
detection of longitudinal magnetization recovery. The second
part of the interleaved data is curve fit to extract the R1
relaxation rate constant and steady state NOE intensity,
making possible calculation of the NOE ratio. The new pulse
sequence is validated against individual R1 and NOE
experiments for the protein ubiquitin.
COMPUTATIONAL NMR
143 - 169
Poster 143
Relativistic Effects in Spin-Spin Coupling Constants
Involving Selenium
1
2
2
Leonid Krivdin ; Irina L. Rusakova ; Yury Yu. Rusakov
1
2
MRC Editor, Irkutsk, Russian Federation; A.E. Favorsky
Irkutsk Institute of Chemistry, Irkutsk, Russian Federation
One-bond spin-spin coupling constants involving selenium of
7 different types, 1J(Se,X), X = 1H, 13C, 15N, 19F, 29Si, 31P,
and 77Se, were calculated in the series of 14 representative
compounds at the SOPPA(CCSD) level taking into account
relativistic corrections evaluated both at the RPA and DFT
levels of theory in comparison with experiment. Relativistic
corrections were found to play a major role in the calculation
of 1J(Se,X) reaching as much as almost 170% of the total
value of 1J(Se,Se) and up to 60-70% for the rest of 1J(Se,X).
Acknowledgements. Financial support from the Russian
Scientific Fund (Grant No. 14-13-00215) is acknowledged.
Poster 144
Computational Protocols for 15N and 31P NMR Chemical
Shifts
1
2
2
Leonid Krivdin ; Valentin A. Semenov ; Dmitry O. Samultsev ;
2
2
Sergey V. Fedorov ; Yury Yu. Rusakov
1
2
MRC Editor, Irkutsk, Russian Federation; A.E. Favorsky
Irkutsk Institute of Chemistry, Irkutsk, Russian Federation
The main factors affecting the accuracy and computational
cost of the calculation of 15N and 31P NMR chemical shifts in
the representative series of organophosphorous compounds
and nitrogen-containing heterocycles are examined at the
DFT and MP2 levels. At the DFT level, the best functionals for
the calculation of 31P NMR chemical shifts are those of Keal
and Tozer, KT2 and KT3. Both at the DFT and MP2 levels,
the most reliable basis sets are those of Jensen, pcS-2 or
pcS-3. Relativistic, vibrational and solvent effects are of minor
importance.
Acknowledgements. Financial support from the Russian
Foundation for Basic Research (Grant No. 14-03-00218a) is
acknowledged.
Poster 145
Investigations into the Properties of the Protein Water
Shel
1
2
Erik Zuiderweg ; David Case
1
University of Michigan Medical School, Ann Arbor, MI;
2
Rutgers University, Piscataway, NJ
The rotational correlation time (tc) is a useful parameter to
determine the oligomerization of proteins in solution. Tc is
given by the Stokes-Einstein relationship (SER). However,
when using the literature value for viscosity, the SER does
not follow the experimental data points.
In order to investigate the cause of this discrepancy, we
carried out molecular dynamics simulations on proteins
between 8 and 42 kDa, with 30,000 explicit water molecules.
We find that the viscosity of water at 3-4 Å from the protein
surface is increased by a factor of 1.6 as compared to bulk
water. When using this increased viscosity, the
correspondence with the data points is excellent, suggesting
that we found the culprit for the deviation of the SER.
Poster 146
Spin Label Probability Density Reconstruction from
Pseudocontact Shift Data
1
2
Ilya Kuprov ; Gareth Charnock
1
2
University of Southampton, Southampton, UK; University of
Oxford, Oxford, UK
It is demonstrated that pseudocontact shift (PCS), viewed as
a scalar or a tensor field in three dimensions, obeys an elliptic
partial differential equation with a source term that depends
on the Hessian of the unpaired electron probability density.
The equation enables straightforward PCS prediction and
analysis in systems with delocalized unpaired electrons,
particularly for the nuclei located in their immediate vicinity. It
is also shown that the probability density of the unpaired
electron may be extracted, using a regularization procedure,
from PCS data.
Page 71
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
Poster 147
A General Approach for Simulating Coherent and
Stochastic Averaging under the Magic-Angle Spinning
Conditions
Alexander A. Nevzorov
North Carolina State University, Raleigh, NC
Membrane proteins undergo uniaxial rotational diffusion about
the membrane normal. A rigorous theoretical description of
this effect under the MAS conditions at arbitrary diffusion rates
in the presence of radiofrequency pulses has remained
challenging. A formulation based on the Stochastic Liouville
equation (SLE) allows one to simulate the spectra at arbitrary
spinning and diffusion rates from fully static to fast-motional
limits. Moreover, the relevant superoperators are timeindependent, which allows for a straightforward generalization
to multidimensional experiments. CP-PI dipolar-recoupling
pulse sequence has been used as an example to illustrate our
approach for simulating two-dimensional MAS spectra. The
correlation between bond angles and the scaling of the dipolar
powder patterns due to rotational diffusion allows one to
extract structural and dynamic information.
Poster 148
A Framework to Analyze the Performance of Decoupling
Sequences in MAS Solid-State NMR
Kong Ooi Tan; Vipin Agarwal; Beat Meier; Matthias Ernst
ETH Zurich, Zurich, Switzerland
We present a theoretical framework that can be used to
analyze the performance of arbitrary multiple-pulse
sequences for heteronuclear spin decoupling. In the
framework of operator-based multi-mode Floquet theory, one
can determine the resonance conditions and then derive
general expressions for the non-resonant first-order and
second-order effective Hamiltonians. Following this, the
effective Hamiltonians containing residual terms that lead to
line-broadening can be expressed and generalized in terms of
Fourier coefficients, which are calculated independently for
each decoupling sequences. We will demonstrate this using
examples of low-power decoupling sequences such as
amplitude-modulated XiX (AM-XiX) and its supercycle variant
SC-AM-XiX. Moreover, the effect of chemical-shift offset on
the resonance conditions and scaling of spin interactions will
also be discussed.
Poster 149
Simulating Cross Effect Dynamic Nuclear Polarization
using Dynamic Monte Carlo
Daniel Wisniewski; Alexander Karabanov; Igor Lesanovsky;
Walter Kockenberger
University of Nottingham, Nottingham, UK
Starting from the full Liouville von Neumann master equation
we projected the cross effect (CE-DNP) dynamics into the
Zeeman subspace using adiabatic elimination. The effective
dynamics are classical in form, yet accurately reflect the
quantum-mechanical treatment. Dynamic Monte Carlo (DMC)
was implemented to simulate interactions in various
geometries. Such approach reduces the problem inherent to
small-system simulations - a finite boundary leads to
misleading results. It has also proven most useful in revealing
polarization dynamics, particularly from the core nuclei to the
bulk, where spin diffusion is seen. The DMC simulations
enable one to study the effect of varying simulation
parameters on polarization values in large spin system during
Page 72
evolution and in steady-state, thus indicating effectiveness of
the parameter choice.
Poster 150
A Rigorous and Efficient Method to Reweight
Conformational Ensembles According to Average
Experimental Data
Hoi Tik Alvin Leung; Olivier Bignucolo; Simon Bernèche;
Stephan Grzesiek
Biozentrum, University of Basel, Basel, Switzerland
Due to slight errors in molecular dynamics (MD) force fields,
experimental NMR parameters may not correlate well with
parameters back-calculated from a non-restrained MD
simulation. These errors lead to incorrect populations of the
individual conformations along the MD trajectory. In the
current study, we have developed COPER, an algorithm
based on convex optimisation and the principle of maximum
entropy that calculates these weights in a completely
deterministic and efficient way that is guaranteed to reach the
global minimum of the fit function. This method has been first
applied to the non-restrained MD simulation trajectory of a
nonapeptide to obtain populations of conformations that are
consistent with experimental NMR parameters.
Poster 151
Cayley-Hamilton Propagators for Nuclear Spin Dynamics
Joseph Sachleben
Univ of Chicago, Chicago, IL
Simulating NMR experiments from first principles has become
easier with the development of advanced computer algebra
systems such as Mathematica. These simulations at the most
fundamental level require the results of time dependent
quantum mechanics. Brute force NMR simulations with
computer algebra systems scale poorly with increasing
dimensionality of the spin system. In contrast, we will show
that the propagator can be simplified by using Cayley–
Hamilton theorem, allowing the propagator to be written as a
finite power series of the Hamiltonian. We will also show that
this form of the propagator allows factorization which
demonstrates that the expectation value of any operator-initial
condition combination is a linear combination of fundamental
spectra (or fids).
Poster 152
NESTA-NMR: Efficient and Generalized Processing of
Multidimensional NUS NMR Data
1
2
1
3
Michelle Gill ; Shangjin Sun ; Yifei Li ; Mitchell Huang ;
1
R. Andrew Byrd
1
2
National Cancer Institute, Frederick, MD; University of
3
Cincinnati, Cincinnati, OH; University of California-Berkeley,
Berkeley, CA
NESTA-NMR is a powerful and efficient program for the
reconstruction of non-uniformly sampled (NUS) NMR data that
incorporates multiple regularization methods, including a
novel first-order gradient descent algorithm (NESTA), which
enables convergence in significantly fewer steps than existing
state-of-the-art methods. NESTA-NMR is able to reconstruct
both high dynamic range and standard J-coupled correlation
experiments with a high degree of fidelity. Reconstruction
times for 4D NMR spectra with NESTA-NMR are only a few
hours on desktop hardware. The program features built-in
parallelization and tight incorporation with NMRPipe to
optimize both computational speed and ease of use.
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
Poster 153
Protein Side-Chain Conformation from Sparse NMR Data
Amr F. Fahmy; Gerhard Wagner
Harvard Medical School, Boston, MA
A program for the calculation of side-chain conformations is
presented which takes as input a family of backbone
conformations of a protein as well as distance constraints
among a small fraction of its residues. The distance
constraints are obtained experimentally from perdeuterated
proteins that are selectively labeled. The program computes a
family of structures that have: 1. minimum overall energy, 2.
minimum deviation from the given distance constraints and 3.
Low RMSD structures for test proteins. The program is useful
for computing side-chain conformations when the backbone is
known or in protein docking applications.
Advances
in
non-uniformly
sampled
(NUS)
data
reconstruction algorithms have resulted in improvements in
sensitivity, resolution and time for multi-dimensional spectra.
Performance is enhanced further when pseudo-random
sampling schedules are chosen according to rules that
sample early in the time domain and avoid large gaps. Here
we show reconstruction accuracy of these schedules can be
predicted using a novel score based on the schedule’s point
spread function. Additionally we demonstrate a superior
metric for schedule performance based on a penalty function
derived from the distribution of unsampled points. These
metrics were successful when using multiple reconstruction
algorithms. We have implemented these metrics for schedule
selection at the console and offline. We expect this will further
enhance NUS performance.
Poster 154
Alternative Sampling Densities in Non-Uniform Sampling
D. Levi Craft; Melissa Palmer; Philip Stahlfeld; David Rovnyak
Bucknell University, Lewisburg, PA
Non-uniform sampling (NUS) is more widely practiced, but
many implementations either do not weight the distribution of
samples, or follow exponential sampling densities. Weighting
the sampling density in proportion to the signal envelope
provides intrinsic sensitivity enhancements (MRC, V49, 483491, 2011). However sinusoidal weighting is a compelling
alternative to exponential weighting matched to the signal
decay (JBNMR, V58: 303-314, 2014). We now describe
families of alternative densities as candidates to replace
common exponential NUS weightings. Yielding equal intrinsic
sensitivity to their exponential counterparts, these alternatives
possess improved constraints on line shapes by distributing
more samples beyond 1xT2. An algorithm to generate properly
gapped sampling densities (JBNMR, V58: 303-314, 2014) is
extended, and is also contrasted with deterministic NUS
schedules.
Poster 157
13
Solid-state C NMR Calculations of Chemical Shielding
Tensors in Metastable Magnesium Carbonates
Blake Hammann; Jeremy Moore; Samuel Emery; Nikhil
Dharan; Sophia Hayes
Washington University, St. Louis, MO
Carbon dioxide (CO2) continues to be a widely studied
molecule due to the earth's rising levels of carbon dioxide.
The potential for CO2 to be geologically stored has been one
avenue of interest. These CO2 reactions that occur
underground have been widely studied in the geological
community and have been found to occur with divalent
cations, such as iron and magnesium. The synthesis of the
metastable magnesium carbonates often results in a mixture
of species, which complicates the NMR lineshape. Herein, we
employ the use of two computational packages (CASTEP and
Quantum ESPRESSO) to help elucidate the NMR lineshape
of the metastable magnesium carbonates. We evaluate the
use of the two computational platforms in the characterization
of small inorganic molecules.
Poster 155
Getting it Right the First Time: How CASE Can Save Time
and Money in Total Synthesis
2
2
1
Sergey Golotvin ; Mikhail Elyashberg ; Patrick Wheeler
1
2
ACD/Labs, Toronto, Canada; ACD Moscow, Moscow, RU
Structural information carried by 2D NMR spectra is by nature
complex, fuzzy and incomplete, and can also be contradictory
and ambiguous. So, it is not surprising that highly qualified
and experienced chemists can and do infer erroneous
structures for new compounds(1). These structures must then
be checked, often using total synthesis of both original and
hypothesized (revised) structures. Labor and other expenses
resulting from structural mis-assignments and subsequent reassignments are considerably greater by erroneous original
assignment. This presentation shows multiple examples
where application of a CASE expert system allows chemists
to avoid deducing erroneous structures of new natural
products. Such a program is an engine for logically deducing
all structures (without exception) which meet initial spectrumstructural information and imposed constraints(2).
Poster 158
Resolution and Sensitivity Enhancement by Maximum
Entropy Deconvolution in Multiple Dimensions
Matthew Zambrello; Mark Maciejewski; Adam Schuyler;
Jonathan Helmus; Jeffrey Hoch
University of Connecticut, Farmington, CT
Fourier spectral methods utilize apodization functions to
enhance sensitivity or resolution. Both cannot be obtained
simultaneously because emphasizing the end of a FID to
enhance resolution amplifies noise. Furthermore, linear
deconvolution (dividing the FID by a convolution kernel) is
unstable whenever the kernel has very small or zero values.
Conversely, maximum entropy reconstruction (MaxEnt) is
capable of stable deconvolution because in this inverse
approach the convolution kernel is multiplied by the inverse
FT of the trial spectrum yielding “mock data” for comparison
with measured data. We show that MaxEnt can be exploited
to achieve resolution enhancement without amplifying noise.
The spectral improvements achieved when deconvolution is
simultaneously performed in two dimensions are substantially
greater than deconvolution in a single dimension.
Poster 156
Optimizing Non-uniform Sampling Performance with
Predictive Scores based on Point Spread Function and
Sampled Point Distributions
Scott Robson; Sven Hyberts; Gerhard Wagner
Harvard Medical School, Boston, MA
Poster 159
17
Solid-State O NMR Shifts in Diamagnetic and
Paramagnetic Systems: A Quantum Chemical
Investigation
Amber Rorick; Rahul Khade; Liu Yang; Yong Zhang
Page 73
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
Stevens Institute of Technology, Hoboken, NJ
Oxygen is an important element in many biological
compounds. However, computational studies of solid-state
17
O NMR shifts have significantly lagged behind experimental
investigations. This work reports the first relatively general
17
methods to accurately compute solid-state O NMR shifts in
diamagnetic and paramagnetic systems. The diamagnetic
systems cover various oxygen environments, including
carboxylate acid, phosphine oxide, nitric oxide, amino acid,
and metal-containing systems and the computational results
were found to have a theory-versus-experiment linear
2
correlation coefficient R =0.991. The broad range of
17
experimental O NMR shifts (~10000 ppm) including both
directly and not directly coordinated oxygens were also
2
accurately reproduced with R =0.984. These methods shall
17
facilitate studies of solid-state O NMR properties in many
diamagnetic and paramagnetic systems, particularly biological
systems.
Poster 160
NMRFAM Software for Protein NMR Spectroscopy
Woonghee Lee; Hesam Dashti; Marco Tonelli; Gabriel
Cornilescu; Vincent Chen; Jaime Stark; Hamid Eghbalnia;
William Westler; Eldon Ulrich; John L. Markley
University of Wisconsin-Madison, Madison, WI
National Magnetic Resonance Facility at Madison (NMRFAM)
software integrated with packages developed elsewhere
supports seamless protein data collection, analysis, structure
determination, and validation. ADAPT-NMR enables reduceddimensionality data collection with concurrent probabilistic
chemical shift assignment—a new BEST option accelerates
data collection. Assignments are combined with NOESY data
as input to PONDEROSA-C/S, which picks peaks
automatically, and to ARECA, which uses the NOE
information to validate chemical shift assignments.
PONDEROSA-C/S calculates 3D structures, which are
evaluated by MolProbity, and improved by iterative,
refinement of NOESY peak lists and assignments. Final
refinement is performed in explicit solvent. Results are
formatted for wwPDB deposition. NMRFAM-SPARKY tools
can be used to visualize, revise, and extend picked peaks and
assignments in terms of underlying spectral data.
Poster 161
Improvements in Accelerating Multidimensional NMR and
MRI Experiments Using Iterated Maps
Jared Rovny; Robert Blum; Sean Barrett; J. Patrick Loria;
Gregory Manley
Yale University, New Haven, CT
Accelerating data acquisition with the advantages of fast
Fourier transform (FFT) reconstruction could benefit a wide
variety of magnetic resonance experiments. Here we discuss
advances to our approach for reconstructing multidimensional
NMR spectra from sparsely-sampled time domain data, using
iterated maps [1]. This method exploits the speed of the FFT
algorithm and is done in a deterministic way, by reformulating
any a priori constraints into projections, and then iterating.
Applying the iterated maps method to real 2D NMR data, we
explain the motivation, the specific projections, the benefits of
a `QUasi-Even Sampling, plus jiTter' (QUEST) sampling
schedule, and recent advances in speedup and
understanding. [1] M. A. Frey, Z. Sethna et al., Journal of
Magnetic Resonance v237, 100 (2013).
Page 74
Poster 162
Automatic and Assisted Fitting of 1H-NMR Spectra
1
2
Carlos Cobas ; Stanislav Sykora
1
Mestrelab Research, Santiago De Compostela, Spain;
2
Mestrelab/Extra Byte, Castano Primo, Italy
Extraction of spin system parameters from NMR spectra by
means of “fitting” is a task which has undergone several
distinct cycles of historic development. We are now poised to
initiate a new cycle, better suited for todays’ environment of
high volume throughput and, ever more often, total
automation of data processing. We no longer consider fitting
as a self-standing task and/or a goal upon itself. It should be
primarily a robust and fast tool for other tasks, such as
Automatic Structure Verification (ASV) or fast Computer
Assisted interpretation of spectra. In this poster we tackle
these ideas and present the progress made so far
Poster 163
A Practical Implicit Membrane Potential for NMRRestrained Calculations of Membrane Protein Structures
1
3
2
Ye Tian ; Charles Schwieters ; Stanley Opella ; Francesca
1
Marassi
1
Sanford-Burnham Medical Research Institute, La Jolla, CA;
2
3
University of California, San Diego, La Jolla, CA; National
Institutes of Health, Bethesda, MD
Traditionally, NMR structures are calculated with a simplified
repulsive term to prevent atom clashing. Such treatment
sacrifices important non-bonded interactions. To facilitate
NMR structure calculations in the proper environment we
developed a computationallypractical implicit solvent and
implicit membrane potential for Xplor-NIH. Application of the
solvent potential (EEFx) in NMR-restrained structure
calculations was presented previously; its implicit membrane
counterpart, IMMx, is presented here. The potential is fully
compatible with experimental NMR restraints and provides
significant improvements both in the quality and precision of
the calculated structures. It provides correct embedding of
membrane proteins in lipid membranes, as well as physically
meaningful insights about residue-residue and proteinmembrane interactions.
Poster 164
Optimal Control of Spin Systems with Newton-Raphson
Methods
David Goodwin; Ilya Kuprov
University of Southampton, Southampton, UK
Magnetic resonance systems can be controlled using a set of
discrete electromagnetic pulses. Designing these pulses is
difficult for complicated systems; numerical optimisation
methods can be used to find a maximum overlap between the
desired state and the state produced by the set of pulses, with
the pulse schedule being the parameter of the objective
function of the optimisation problem.
Existing methods are typically based on finding the gradient of
the objective function to converge to a maximum overlap
between states. Using novel mathematical techniques we
found a more efficient algorithm, scaling with O(n), to
calculate the matrix of second derivatives needed for a
Newton-Raphson method, a method having better
convergence properties than that of gradient descent and
quasi-Newton methods.
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
Poster 165
An Experimental and Computational Platform for HighThroughput Structural Characterization of Families of
Proteins
1
1
2
Jonas Fredriksson ; Martin Billeter ; Fabio Almeida
1
University of Gothenburg, Gothenburg, Sweden;
2
UFRJ, Rio De Janeiro, Brazil
We demonstrate a complete characterization with the
projection-decomposition approach of the small protein hbd6,
including backbone, side chain assignments and a structure
determination. After the decomposition of 4D HCC(CO)NNH
and 15N-HSQC-NOESY-15N-HSQC it is necessary to pair
each HC with its C (TOCSY) and HN with N (NOESY). This is
achieved by a novel approach called “TILT”, where a second
decomposition using a coordinate system where the axes HC
and C (HN and N) are rotated 45°. This approach yields, with
one exception, complete and correct assignments of the
aliphatic side chain groups. For the NOESY, TILT results in a
complete set of short distances. A well-defined structure was
calculated with a backbone RMSD to its mean of 1.0 Å.
Poster 166
Joint Inversion of NMR T1-T2 Spectrum Combining the
Iterative TSVD and the Parallel PSO Algorithms
Xinmin Ge
China University of Petroleum, Qingdao, China
We introduce a joint method to inverse the T1-T2 spectrum,
which combines the iterative truncated singular value
decomposition (TSVD) and the parallel particle swarm
optimization (PSO) algorithms to get fast computational speed
and stable solutions. We reorganize the first kind of Fredholm
integral equation of two kernels to a nonlinear optimization
problem with non-negative constraints, and then solve the illposed problem by iterative TSVD. Truncating positions of the
two diagonal matrices obtained by the Akaiake information
criterion. PSO is then implemented to get the global optimal
solutions with initial values obtained by TSVD. Parallel
structure is adopted to speed up the computation time. The
performance of the proposed method is validated by synthetic
data with different SNRs.
Poster 167
Optimizing NUS Sampling Strategy and Reconstruction
Based on Extensive Simulation
Sven G. Hyberts; Scott Robson; Gerhard Wagner
Harvard Medical School, Boston, MA
We question what is the optimal sampling length without
previous assumptions. We sample 512 complex data points
in various fashions that have been selected from 4 different
synthetic FIDs consisting of 4096 complex points and
exponentially damped ending at tmax of 1*T2, 2*T2, 3*T2 and
4*T2, respectively. We apply different sets of noise with the
same power and reconstruct to equal digital resolution. The
resulting spectra are picked with the NMRDraw peak picker,
and the results are analyzed for (a) resulting average peak
height for best sensitivity, (b) resulting standard deviation of
the peak position for frequency accuracy, and (c) resulting
average line width for resolution to avoid signal overlap.
Poster 168
nD-PDPA: A Method for Structure Refinement Using
Unassigned Residual Dipolar Couplings
Arjang Fahim; Homayoun Valafar
University of South Carolina, Columbia, SC
The characterization of a protein, is expensive and time
consuming regardless of novelty of the target protein.
Probability Density Profile Analysis (PDPA) has been
previously introduced by our lab to directly address the
economies of structure determination of routine proteins and
subsequently, identification of novel structures from minimal
set of RDC data. Here we present the latest version of the
software nD-PDPA that utilizes more than two sets of nonuniform (e.g N-H and C-H), unassigned RDC sets from
different alignment media to identify the most appropriate
computed structure of an unknown protein. In addition, we
have developed a protocol to refine an unknown protein,
utilizing experimental RDC sets to produce a closer structure
to the unknown protein.
Poster 169
Data Mining PubChem in Search of Compound Families
with Similar NMR Data
1
2
Gonzalo Hernández ; Fabrice Moriaud ;
2
2
Bjoern Heitmann ; Till Kuehn
1
2
Vis Magnetica, Montevideo, Uruguay; Bruker BioSpin AG,
Faellanden, Switzerland
We are interested in understanding NMR data diversity from
known small organic molecules. While chemical structure
diversity can be measured by enumerating all possible
structures for a given molecular formula, their NMR data is
very difficult to obtain, either experimentally or
computationally.To overcome this obstacle, we have used the
MolSimNMR similarity calculation method in order to cluster a
subset of 2 million small organic molecules from PubChem
into compound families expected to present very high NMR
1
1
13
data similarity for H-1D and H- C HSQC experiments.In this
poster, we present the results of this work and discuss
possible applications ranging from database search,
compound classification, and NMR prediction.
MRI / MRS
170 - 209
Poster 170
Practical Optimized Phase-Sensitive Inversion Recovery
for MRI Contrast Enhancement
1
2
3
1
Yan Chang ; Daxiu Wei ; Steffen Glaser ; Xiaodong Yang
1
2
SIBET, Chinese Academy of Sciences, Suzhou, China; East
3
China Normal University, Shanghai, China; Technische
Universitaet München, Garching, Germany
Suppression of tissues with given T1 values, also known as
saturation contrast, has already been widely used in selective
signal nulling for cerebrospinal fluid or fat. It indicates that the
tissue contrast can be increased by using doubled dynamic
range of longitudinal magnetization with a proper ratio of
TI/T1, which also referred as phase-sensitive inversion
recovery (PSIR). We show that this contrast can be further
increased with an optimal inversion pulse, which is optimized
by an extended version of optimal-control-based gradient
ascent (GRAPE) method. The new approach is denoted as
POP-SIR (Practical Optimized Phase-Sensitive Inversion
Recovery), and it has a great potential for enhancing contrast
of tissues, and in particular, of limited intrinsic different
tissues.
Page 75
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
Poster 171
A Method for Improving the Quality of Magnetic
Resonance Imaging through Dynamic Gain Adjustment
Weimin Wang; Yuanyuan Liu
Peking University, Beijing, China
An efficient method for improving the quality of magnetic
resonance imaging (MRI) by reducing quantization noise is
proposed in this paper. In this method, the receiver gain is
dynamically adjusted according to the amplitudes of signals
before each acquisition of the echo signal in different phase
encoding steps, which maximizes the utilizable data bits in
digitization, and reduces quantization noise. The proposed
method does not incur additional costs of hardware. Scanning
experiments were carried on phantoms and human heads
using a 1.5T superconductive MRI system. Experimental
results demonstrate that the proposed method is able to
improve not only the signal-to-noise (SNR) ratio and but also
image details.
Poster 172
Comparison of CEST Effects from Common Metabolites
with Varying External Fields and pH in vitro
1
1
2
Jae-Seung Lee ; Ding Xia ; Alexej Jerschow ;
1
Ravinder Regatte
1
Radiology Department, New York University, New York, NY;
2
Chemistry Department, New York University, New York, NY
Chemical exchange saturation transfer (CEST) provides
contrast mechanisms for the amplified detection and
monitoring of biomarkers and physiologically active
molecules. In biological tissues and organs, many
endogenous CEST agents coexist, and their CEST effects
often overlap. Characterizing individual CEST effects from
different metabolites would be useful for interpreting such
overlapped CEST effects and for designing new CEST
applications. Here we performed an in vitro study to evaluate
individual CEST effects arising from common metabolites
found in biological tissues and organs at 3 T, 7 T, and 11.7 T.
The CEST effects were compared in consideration of the
exchange regime and the acidity of the exchangeable protons.
Poster 173
Evidence for Alignment of Sodium Nuclei in Spinal Cord
by the Magnetic Field
Uzi Eliav; Gil Navon
School of Chemistry, Tel Aviv University, Tel Aviv, Israel
In the present work, performed on spinal cord, we address the
23
question whether the order presented by spectra of Na in
this tissue is defined on local or macroscopic levels and
whether it depends on the orientation of the sample in respect
to the magnetic field. It is shown that some of the sodium
nuclei present spectra characteristic of macroscopic order. It
was found to be independent of the sample orientation in
respect to the magnetic field. This suggests that the magnetic
field may play a role in the sodium alignment that needs
further studies.
Poster 174
Altered Antioxidant Profile in the Healthy Elderly Occipital
and Posterior Cingulate Cortices
1
Measured via 7 T H MRS
1
2
2
Malgorzata Marjanska ; J. Riley McCarten ; Laura Hemmy ;
1
1
Dinesh Deelchand ; Melissa Terpstra
1
2
CMRR, University of Minnesota, Minneapolis, MN; GRECC,
Minneapolis VA Medical Center, Minneapolis, MN
Page 76
Oxidative stress occurs at an early stage of age related
cognitive decline. Ascorbate (Asc, vitamin C) and glutathione
(GSH) are key contributors to the antioxidant network. We
1
utilized short echo time H MRS at 7 T to reliably quantify
these antioxidant concentrations in the aging brain in the
occipital cortex and the posterior cingulate cortex, which is
pertinent to the pathology of Alzheimer’s disease. Asc was
higher and GSH lower in elder subjects in both brain regions.
The Asc difference in the PCC were the most significant (p =
-5
1.8 x 10 ). This work has important implications for ongoing
development of antioxidant based diagnosis, prevention and
treatment of cognitive decline.
Poster 175
Virtual Phantom for Magnetic Resonance Imaging of
Water-Lipid Systems
1, 2
1
Roberto Salvati ; Jean-Jacques Bellanger ; Giulio
1, 2
1, 3
Gambarota ; Hervé Saint-Jalmes
1
2
Université de Rennes 1, LTSI, Rennes, France; INSERM,
3
U1099, Rennes, France; Centre Eugène Marquis,
Rennes, France
Virtual Phantom (ViP) for MRI is a method to generate
reference signals, without using physical objects: given a
numerical phantom, a waveform generator converts the kspace lines into a radiofrequency signal that is transmitted to
the scanner by an RF coil. The scanner records the ViP signal
simultaneously as the signal from the object of interest. In the
previous work it was shown that ViP MRI could substitute real
phantoms, using magnitude images. The aim of this study is
to test the ViP MRI method to generate complex (magnitude
and phase) images that mimic water-lipid systems in the
presence of virtual magnetic field inhomogeneities. To this
aim, multi gradient-echo images of ViPs and physical
phantoms were acquired and reconstructed.
Poster 176
On the Origin of Changes in CEST Effects upon Protein
Unfolding: Quantitative Evaluation of Exchange Rates
and Relative Proton Fractions
Steffen Goerke; Moritz Zaiss; Patrick Kunz;
Karel D Klika; Peter Bachert
German Cancer Research Center, Heidelberg, Germany
To pave the way towards a selective detection of global
protein folding states by Chemical Exchange Saturation
Transfer (CEST) imaging we previously employed a
comprehensive spectral signature of protein unfolding. Since
the origin of these characteristic signal changes remained
unclear, we investigated quantitatively the changes in
exchange rates and relative proton fractions by Water
Exchange (WEX) spectroscopy and a novel multiple-B1 CEST
data evaluation approach. Remarkably, exchange rates tend
to remain constant upon protein unfolding. Instead the
observed signature of protein unfolding rather originates
mainly from variations of the relative fraction of protons
detectable by CEST. A CEST method less sensitive to
changes in exchange rates could therefore enable a selective
detection of protein unfolding.
Poster 177
Low-Cost High-Performance MRI
1, 2
1, 2
1, 2
Mathieu Sarracanie ; Cristen LaPierre ; Najat Salameh ;
1, 3
1
1, 2
David Waddington ; Thomas Witzel ; Matthew Rosen
1
MGH/A.A. Martinos Center for Biomedical imaging,
2
Charlestown, MA; Department of Physics, Harvard
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
3
University, Cambridge, MA; School of Physics, University of
Sydney, Sydney, Australia
MRI is unparalleled in its ability to non-invasively visualize
anatomical structure and function with high spatial and
temporal resolution and a broad range of clinical contrasts.
The vast majority of clinical scanners incorporate
superconducting magnets operating at 1.5, 3 and more
exceptionally at 7T. At 6.5 mT, more than 450x lower than
clinical MRI scanners, we demonstrate 2.5×3.5×8.5 mm^3
resolution in the living human brain in 6 minutes. We contend
that robust non-field-cycled low-field implementations of MRI
(< 10mT) have the potential to make clinically relevant images
and set new standards for a completely new category of
affordable robust portable device.
Poster 178
3D Balanced-EPI Magnetic Resonance
Fingerprinting at 6.5 mT
1, 2
1
1, 2
Mathieu Sarracanie ; Ouri Cohen ; Matthew Rosen
1
MGH/A.A. Martinos Center for Biomedical Imaging,
2
Charlestown, MA; Department of Physics,
Harvard University, Cambridge, MA
2D MR Fingerprinting has recently been shown at low
magnetic field. Here, we demonstrate MRF in 3D at 6.5 mT,
using an optimized set of 15 flip angles and repetition times
(FA/TR), in a Cartesian acquisition of k-space with a new
hybrid b-SSFP-EPI sequence. We measure quantitative
parameters in 3D, and generate several image contrasts in a
single acquisition (proton density, T1, T2) in less than 30
minutes. The combination of 3D MRF with low field MRI
scanners has great potential to provide clinically relevant
contrast with portable low cost MR scanners.
and Technology, Cambridge, MA;
5
EPFL, Lausanne, Switzerland
MR elastography cannot be performed in subjects with iron
overload due to both a dramatic drop of signal on the MR
images, and strong magnetic susceptibility artifacts. We
propose in this work an alternative to biopsy for patients with
chronic liver diseases where MRE has already shown its
robustness in staging liver fibrosis and even in the diagnosis
of steatohepatitis before fibrosis appears. For that purpose,
we implemented a high performance MRE sequence on a 6.5
mT scanner. We successfully performed MRE in samples
prepared with different iron content and compared our
performance to standard clinical 1.5 T scanners.
Poster 181
Fast in-vivo Magnetic Resonance Fingerprinting with
Cartesian Sampled Spin-Echo Echo-Planar-Imaging
1
1, 2
1, 2
Ouri Cohen ; Mathieu Sarracanie ; Matthew Rosen ;
1
Jerome L. Ackerman
1
MGH/A.A. Martinos Center for Biomedical Imaging, Boston,
2
MA; Department of Physics, Harvard University,
Cambridge, MA
Magnetic resonance fingerprinting uses a random set of flip
angles (FA) and repetition times (TR) to simultaneously
sensitize a scan to multiple tissue properties. In previous work
we described an optimization method that allows significant
reduction (2 orders of magnitude) in the required number of
acquisitions. In this work we demonstrate an application of our
method using a Cartesian, fully sampled, spin-echo planar
imaging (SE-EPI) sequence to acquire multiple tissue maps
from a single slice in 7 seconds on a clinical 1.5 T scanner.
Poster 179
Selective Dynamical Recoupling of Diffusion-Driven
Decoherence: Magnetic Resonance Imaging Applications
Gonzalo Agustin Alvarez; Noam Shemesh; Lucio Frydman
Weizmann Institute of Science, Rehovot, Israel
Dynamical decoupling, a generalization of the original NMR
spin-echo sequence, is becoming a relevant tool for reducing
decoherence in quantum systems. One such sequence,
Selective Dynamical Recoupling (SDR) allows one to filter out
“intrinsic” T1 and T2 effects, as well as pulse-errors acting as
additional sources of decoherence. Here, we describe how
such features can be exploited to selectively address spin
signal decays driven by molecular diffusion effects. The
ensuing methods provide a tool to measure restriction lengths
in confined porous systems. SDR-based Non-uniform
Oscillating-Gradient Spin-Echo sequences enable the
mapping of compartment sizes and their distributions in
important MR imaging settings. SDR presents unique ways of
probing internal magnetic field gradients and their distributions
for mapping orientations in Biological tissues.
Poster 182
Hollow Fe/Gd Mixed Oxide Nanorings as T1 and T2 DualModality MRI Contrast Agents
1
2
1
Yu-Wen Chen ; Deepak Verma ; Chia-Hau Cheng ; Anil K.
2
1
Sinha ; Dennis Hwang
1
Dpet. of Chem. & Biochem, National Chung Cheng Uni,
2
Chia-Yi, Taiwan; CSIR-Indian Institute of Petroleum,
Dehradun, India
Contrast enhancement can be fulfilled through the use of
contrast agents (CAs). Therefore, designing a CA to enhance
relaxivity would be beneficial. In this study, we present new
dual-modality T1 and T2 CAs based on hollow Fe/Gd oxide
nanorings. According to the NMR dispersion (NMRD) profiles,
the relaxation process of these nanorings mixes both IS and
OS relaxations. In addition, both the T1 and T2 relaxation of
this new CA are significantly affected by the molecular
motions of water. Furthermore, since this new CA shows fast
T1 and T2 relaxation, a novel contrast in the phantom image
was demonstrated by simple post-processing of T1 and T2
mapping images to identify the region wherein the Fe/Gd
oxide nanorings conducted.
Poster 180
Magnetic Resonance Elastography in the
Presence of Iron Overload
1, 2
1, 2
1
Najat Salameh ; Mathieu Sarracanie ; Christian Farrar ;
1, 3
5
1, 4
David Waddington ; Arnaud Comment ; Bo Zhu ;
1, 2
Matthew Rosen
1
MGH/A.A. Martinos Center for Biomedical Imaging,
2
Charlestown, MA; Department of Physics, Harvard
3
University, Cambridge, MA; School of Physics, University of
4
Sydney, Sydney, Australia; Harvard-MIT, Health Sciences
Poster 183
Biodetection by Fast-Field Cycling NMR Relaxometry
Chia-Ying Lee; Dennis Hwang; Yu-Wen Chen
Dpet. of Chem. & Biochem, National Chung Cheng Uni,
Chia-Yi, Taiwan
MRI contrast agents are important in clinical applications.
They are applied on many disease and tumor detections as a
non-invasive agent . They also can be used for in vitro
biodetection. When macromolecules, such as protein and
antibody, bind to gadolinium(III) based contrast agents, it
Page 77
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
changes the molecular weight and makes the rotational
correlation time of proton becomes longer. Consequently, it
influences the magnetic resonance dispersion profiles , which
can be used for biodetection. In this study, Gd-DOTA-GA was
used as a contrast agent. DOTA-GA contains anhydride
groups which can react with the amino groups on antibody
and protein and then this open ring process offer a carboxyl
group which can stabilize the Gd3+ chelated.
Poster 184
Design and Evaluation of a Flexible, Modular Biosensor
129
for Xe Hyper-CEST MRI
1
1
1
Honor Rose ; Christopher Witte ; Federica Rossella ; Stefan
1
2
1
Klippel ; Christian Freund ; Leif Schröder
1
2
FMP, Berlin, Germany; Freie Universität Berlin,
Berlin, Germany
Xenon Hyper-CEST MRI utilizes the interaction of
hyperpolarized xenon with specialized host molecules (e.g.
Cryptophane A (CrA)) to create highly sensitive biosensors.
This novel class of biosensors has the potential to detect
cellular targets of much lower abundance than conventional
MRI contrast agents. We designed a dual-functional
(fluorescence and CrA-containing), modular xenon biosensor
which facilitates quick and easy adaptation to any cell surface
target for which there is a specific antibody. As an example
we demonstrate, in cellulo, a biosensor with which we can
image cells expressing the surface protein CD14 with CrA
concentrations as little as 20 nM. Such a flexible and modular
biosensor should prove an efficient tool for evaluating a
multitude of future targets with ease.
Poster 185
129
Referenced Lipid-Dissolved Xe MR Thermometry
1, 2
2, 3
2, 3
Le Zhang ; Alex Burant ; Drew McCallister ; Karl M.
4
2, 3
Koshlap ; Rosa Tamara Branca
1
Department of Applied Science and Engineering, UNC
2
Chapel Hill, Chapel Hill, NC; Biomedical Research Imaging
3
Ctr, UNC Chapel Hill, Chapel Hill, NC; Dept of Physics and
4
Astronomy, UNC Chapel Hill, Chapel Hill, NC; Eshelman
School of Pharmacy, UNC Chapel Hill, Chapel Hill, NC
We explored the effects of microscopic susceptibility gradients
on the methylene-referenced PRF thermometry and proposed
a new method utilizing temperature dependence of the
129
Xe (LDX). Simulation and
chemical shift of lipid-dissolved
ex vivo spectroscopic results on various fat-rich tissue
samples showed great variations in referenced PRF method,
but much improved consistency when chemical shift of LDX
was referenced to the methylene peak of lipid spins residing in
the same compartment. Although LDX-methylene method
129
Xe, preliminary
also exhibited dependence on pressure of
pressure study showed a threshold well above those
obtainable in vivo. This suggests that LDX-methylene method
could be used as an absolute temperature probe.
Poster 186
Quantitative CEST (qCEST) using Ω-plots in the Case of
Trains of Gaussian-shaped Saturation Pulses
1
1
1
Jan-Eric Meissner ; Moritz Zaiss ; Steffen Goerke ; Eugenia
1
2
1
1
Rerich ; Alexander Radbruch ; Mark E Ladd ; Peter Bachert
1
German Cancer Research Center, Heidelberg, Germany;
2
University of Heidelberg Medical Center,
Heidelberg, Germany
The contrast in CEST imaging experiments depends on the
concentration of exchanging protons, and on their exchange
Page 78
rate. Recent studies showed that the Ω–plot method is able to
quantify both parameters simultaneously in the case of
continuous wave (cw) saturation. We propose an advanced
Ω–plot method that enables the quantitative determination on
SAR-limited whole-body scanners, where only pulsed
saturation is possible. Our extension includes form factors to
correct for the Gaussian-shape of our pulses. This yields
improved estimation of quantitative values for both
parameters up to exchange rates of several thousand hertz in
solutions, but is in principle also applicable in vivo.
Poster 187
In vivo Quantification of Iron Oxide Nanoparticle
Biodistribution using Positive T1 Contrast
1
1
2
3
Hattie Ring ; Jinjin Zhang ; Katie Hurley ; Qi Shao ; Christy
2
3, 4
1
Haynes ; John Bischof ; Michael Garwood
1
Center for Magnetic Resonance Research, U of MN,
2
Minneapolis, MN; Department of Chemistry, University of
3
Minnesota, Minneapolis, MN; Department of Biodmedical
4
Engineering, U of MN, Minneapolis, MN; Department of
Mechanical Engineering, U of MN, Minneapolis, MN
Iron oxide nanoparticles (IONPs) have much potential for
cancer therapy and biopreservation applications. To further
advance in vivo IONP applications, a clinical imaging
technique capable of non-invasively quantifying IONP
distribution is required. We investigate the distribution of
IONPs injected in mice intratumorally and intravenously using
the T1 contrast measured with sweep imaging with Fourier
transformation (SWIFT). SWIFT is a relatively new pulse
sequence with short (~7 µs) delay between excitation and
acquisition, which allows it to preserve signals from spins with
*
extremely short T2 , such as IONPs. Combining SWIFT with
Look-Locker R1 mapping, IONP concentrations as high as 1.9
mg Fe/g tissue are quantified.
Poster 188
Creatine Concentration in Human Calf Muscle at 7T with
AREX
Eugenia Rerich; Moritz Zaiss; Johannes Windschuh;
Patrick Schuenke; Peter Bachert
German Cancer Research Center, Heidelberg, Germany
Creatine is an important compound in the energy metabolism
of cells. Non-invasive detection of creatine in living tissue can
be realized via attenuation of the bulk water signal following
proton exchange (CEST). Recently it was shown that
endogeneous CEST contrasts are strongly affected by the MT
background as well as by T1 relaxation of the water protons.
This influence can be corrected in the Z–spectrum by a
method that yields the apparent exchange–dependent
relaxation (AREX). AREX has some useful linearity features
which
enable
preparation
of
almost
independent
concentration–weighted CEST contrasts. In this study AREX
was applied to in vivo CEST imaging data of the human calf
muscle before and after exercise and showed an increase of
the creatine level upon muscle activity.
Poster 189
Application of Calibrationless Parallel Imaging
13
Reconstruction to Hyperpolarized C MRI for Clinical
Applications
1
1
1
2
Yesu Feng ; Jeremy Gordon ; Peter Shin ; Michael Lustig ;
1
1
1
Peder Larson ; Cornelius Morze ; Michael Ohliger ; Lucas
1
3
1
Carvajal ; James Tropp ; Daniel Vigneron
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
1
2
3
UCSF, San Francisco, CA; UC Berkeley, Berkeley, CA; GE
Healthcare, Fremont, CA
13
Hyperpolarized (HP) C imaging requires fast data acquisition
due to the fast T1 relaxation and nonrenewable nature of the
hyperpolarized magnetization. Parallel imaging methods are
well suited for acceleration of data acquisition, yet
conventional parallel imaging schemes require explicit
estimation of coil sensitivity which presents significant
13
challenge to HP C imaging. In this study, a calibrationless
parallel imaging method called simultaneous auto-calibrating
and k-space estimation (SAKE) was developed and applied to
13
HP C MRI. This technique requires no a priori knowledge of
coil sensitivity and achieved a 2-fold acceleration when
combined with 2D EPI readout. This strategy can be readily
translated for clinical study and can be combined with other
acquisition schemes such as multi-slice and non-Cartesian
acquisitions.
Poster 190
Monitoring Iron in Metabolic Prostate Cancer Therapy
*
with T2 MRI Relaxometry
Avigdor Leftin; Jason Koutcher
Department of Medical Physics, Memorial Sloan Kettering
Cancer Center, New York, NY
Citrate, a metabolic prostate cancer biomarker, is regulated by
3+
the Fe -dependent mitochondrial enzyme m-aconitase. Maconitase inhibition with the iron-chelator deferiprone is a
promising metabolic prostate cancer therapy. To monitor
*
tumor growth and systemic drug delivery, a T2 relaxometric
3+
quantification and tumor
MRI protocol enabling Fe
measurement was implemented. We combined these
relaxometric measures with in vivo magnetic resonance
spectroscopy, immunohistochemistry, and high-resolution
NMR of tissue culture and tumor tissue metabolites to
characterize the pathological and metabolic effects of
deferiprone in an orthotopic murine Myc-CaP prostate cancer.
The results indicated that deferiprone has anti-neoplastic
3+
effects in prostate tumors, reduces hepatic Fe load in
response to oral gavage, and alters metabolism of prostate
cancer in this mouse model.
Poster 191
Doublet GABA Editing with Frequency Insensitive
Macromolecule Suppression using
MEGA-SPECIAL Sequence
1
2
3
4
Meng Gu ; Ralph Hurd ; Ralph Noeske ; Ariel Rokem ; Laima
5
1
Baltusis ; Daniel Spielman
1
2
Radiology, Stanford University, Stanford, CA; GE
3
Healthcare, Menlo Park, CA; GE Healthcare, Berlin,
4
Germany ; Psychology, Stanford University, Stanford, CA;
5
Center for Cognitive and Neurobiological Imaging,
Stanford, CA
Doublet
GABA
editing
with
frequency-insensitive
macromolecule suppression using MEGA-SPECIAL sequence
has been developed. By using a very frequency-selective
editing pulse with a reduced flip angle of 135º, the center peak
contributions to the 3ppm GABA resonance are reduced to
obtain a clear doublet. Macromolecule was suppressed using
this editing pulse without applying a lysine-symmetric editing.
Phantom spectra demonstrated a clean edited GABA doublet.
Using the lysine-symmetric method as a reference, in-vivo
studies showed a GABA doublet resonance can be obtained
with MM suppression. As the residual macromolecule signal is
not expected to be a simple pseudo-doublet and can be
discriminated from GABA. The edited GABA doublet can thus
be fitted with a doublet for improved quantification.
Poster 192
MRI Study of Tissue Protein and Lipid Content using
Pulsed Magnetization Transfer
Jeff Duyn; Xu Jiang; Peter van Gelderen
NIH, Bethesda, MD
Use of a pulsed magnetization transfer (MT) technique is
proposed to measure the fraction f of not-water hydrogen
protons in-vivo, and infer loss of brain myelin resulting from
disease. Using an optimized RF pulse operating within the
power constraints of clinical MRI scanners, the magnetization
of 1H protons on proteins and lipids is selectively saturated,
after which the transfer of this saturation to 1H water protons
is measured with a gradient echo (GRE) EPI sequence.
Reliable extraction of f and magnetization transfer rate
constant k between non-water and water 1H protons was
possible with scan times as short as 5 minutes using 2-pool
model of MT.
Poster 193
F-MRS Assessment of Tissue-Engineered
Graft Oxygenation
1
1
2
Samuel Einstein ; Bradley Weegman ; Thomas Suszynski ;
1
1
1
Meri Firpo ; Melanie Graham ; Lynn Eberly ; Klearchos
3
1
Papas ; Michael Garwood
1
2
University of Minnesota, Minneapolis, MN; University of
Texas Southwestern Medical Center, Dallas, TX;
3
University of Arizona, Tucson, AZ
Tissue-engineered grafts (TEGs) containing islets have the
potential to cure diabetes. Maintaining an adequate partial
pressure of oxygen (pO2) within TEGs is critical, as both
hypoxia and anoxia are detrimental to islet function and
survival. The spin-lattice relaxation rate, R1 (=1/T1), of
perfluoro-15-crown-5-ether has previously been demonstrated
19
to be sensitive to pO2. F-MRS-based relaxometry was
adapted to measure TEG pO2 and successfully validated with
fiber optic (FO) probes. The pO2 in TEGs and control TEGs
(without islets) implanted into a subcutaneous pocket of a rat
19
were measured with F-MRS and additionally validated with
FO probes. Implanted TEGs were found to be hypoxic, but we
demonstrated in vivo that supplying the TEG with
supplemental oxygen gas can increase the TEG pO2.
In vivo
19
Poster 194
A Robust T1ρ-Mapping Method Feasible for in-vivo
Glucose Detection at 7T Whole-Body Scanners
Patrick Schuenke; Moritz Zaiss; Peter Bachert
German Cancer Research Center, Heidelberg, Germany
Chemical exchange sensitive spin-lock allows measuring the
uptake of administered D-glucose in-vivo and therefore could
be an interesting, non-invasive technique for tumor imaging.
To overcome the problem of artifacts induced by
inhomogeneities in the B0 and B1 field, which are common
problems especially at high-field whole-body scanners, we
implemented an adiabatic spin-lock sequence which is
compatible with the strict SAR-limitations of human MR
scanners and provides a sufficient temporal resolution. We
could show that our sequence outperforms a classical spinlock sequence with respect to the insensitivity to B1 fieldinhomogeneities in-vitro as well as in-vivo. Further the
sensitivity to changes in glucose concentration in the
Page 79
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
millimolar range was proven so that the method is ready for
use in clinical trials.
Poster 195
Characterization of the Evolving Neuropathology in the
Hippocampal Formation of the 5xFAD Mouse Model of
Alzheimer's Disease
Palamadai Venkatasubramanian; Benjamin Banks; Kaushik
Govindaraju; George Iordanescu; Alice Wyrwicz
NorthShore Univ. HealthSystem, Evanston, IL
The differential effects of Alzheimer’s disease (AD) on the
interconnected subfields of the hippocampal region need to be
better characterized in the early stages of the disease in order
to understand how the progression of neuropathology impacts
the major hippocampal circuits. We have investigated the
cytoarchitecture of the hippocampus in the 5xFAD transgenic
mouse model of AD using high resolution morphological
imaging, and found layer-specific changes within the dentate
gyrus (DG) and CA1 at different stages of amyloid pathology,
indicating possible differential alterations of these two main
circuits during evolving neuropathology.
Poster 196
The Power of a CEST Evaluation Metric Independent of
Water Relaxation
1
1
2
2
Moritz Zaiss ; Steffen Goerke ; Hua Li ; John C. Gore ; Mark
1
1
2
E. Ladd ; Peter Bachert ; Junzhong Xu
1
German Cancer Research Center, Heidelberg, Germany;
2
Vanderbilt Institute of Imaging Sciences, Nashville, TN
Chemical exchange saturation transfer (CEST) of metabolite
protons that undergo exchange processes with the water pool
enables a specific contrast for magnetic resonance imaging
(MRI). However, as mediated by the water pool, CEST effects
as typically evaluated show a strong dependence on the water
longitudinal relaxation time. Herein we present the power of
the inverse metric evaluation, which yields robust estimation
of CEST effects independent of water relaxation changes. By
this we could show that NOE-CEST effects, originating from
aliphatic protons, have no direct dependence on water T1
even though NOE and T1 relaxation are similar processes.
Finally, the power of this metric is that in vivo CEST
measurments can be performed also in the presence of Gd
contrast agents.
Poster 197
Rhesus Macaque Cerebral Cortical Diffusion Anisotropy
in utero: Cortical Folding but Not Surface Area Expansion
Scale with Cellular Morphological Differentiation
1
2
1
Xiaojie Wang ; Colin Studholme ; Christopher Kroenke
1
2
OHSU, Portland, OR; University of Washington, Seattle, WA
Recent advances in fetal MRI have enabled the measurement
of water diffusion anisotropy in brain tissue in utero. In order
to
characterize
the
relationship
between
cellular
morphological maturation in the cerebral cortex and
macroscopic aspects of brain development, we performed
diffusion MRI on brains of five rhesus macaque fetuses
longitudinally at three gestational ages (G85, G110, and G135
of a 165 day term). We find that correlations between diffusion
anisotropy and cerebral cortex surface area expansion are
weaker than previously predicted based on cross-sectional
analyses of tissue post mortem. However, unexpectedly
strong correlations between diffusion anisotropy and cerebral
cortical folding are observed.
Page 80
Poster 198
129
Hyperpolarized Xe Diffusion MRI of COPD Rats
Jianping Zhong; Weiwei Ruan; Xianping Sun; Chaohui Ye; Xin
Zhou
Wuhan Inst. of Physics and Mathematics, CAS,
Wuhan, Hubei, China
129
The measurement of
Xe ADC in rat lungs is facing
challenges due to the small tidal volume and low SNR. We
129
Xe diffusion-weighted MRI
used a new hyperpolarized
2
method with a single b value ( b=14 s/cm ) for higher image
129
SNR in COPD rat models. The lung parenchymal Xe ADC
distribution maps of COPD rats were obtained on a 7.0 T MRI
scanner. The mean lung parenchymal ADC of
2
0.04422/0.04234 cm /s (Δ=0.8/1.2 ms) for COPD rats showed
a significant increase compared to that of 0.0377/0.0367
2
cm /s (Δ=0.8/1.2 ms) for healthy rats(p=0.0079/0.0053 for
Δ=0.8ms/1.2ms), consistent with the alveolar airspace
enlargement in COPD rats according to the H&E-stained
histology.
Poster 199
Quantitative Evaluation of Pulmonary Gas-Exchange
Using Chemical Shift Saturation Recovery with Different
Excitation Pulses Time (CSSR-DEPT)
Zhiying Zhang; Haidong Li; Xiuchao Zhao; Xianping Sun;
Chaohui Ye; Xin Zhou
Wuhan Inst. of Physics and Mathematics, CAS, Wuhan,
Hubei, China
Gas exchange is the most essential function of lung.
Hyperpolarized Xe MR is one of the rare techniques capable
of providing gas exchange function quantitatively. The fluidity
of blood is critical in air-blood exchange analysis and makes
the simulation difficult. A modified chemical shift saturation
recovery sequence with different excitation pulse time (CSSRDEPT) was chosen to study the dynamics of xenon in lung.
The air-blood exchange function between healthy and dead
rat was compared to reveal the influence of blood flow on airblood exchange. The influence of blood flow on gas uptake
was demonstrated and the gas exchange time constant
reduced when the blood flowed. The FWHM of dissolved Xe
narrowed when the blood flow stopped.
Poster 200
Multiband RF Pulse with Improved Performance via
Convex Optimization
1
1
2
3
Hong Shang ; Peder E. Z. Larson ; Adam Kerr ; Galen Reed ;
1
1
4
Adam Elkhaled ; Jeremy Gordon ; Michael Lustig ;
1
Daniel Vigneron
1
2
UCSF, San Francisco, CA; Stanford University, Stanford,
3
4
CA; HeartVista, Menlo Park, CA; UC Berkeley, Berkeley, CA
A framework for general RF pulse design is developed using
convex optimization. It can create RF pulse with multiband
magnitude profile, arbitrary phase profile and generalized flip
angle. Spectral profile sparsity is exploited to further optimize
some characteristics, such as duration, transition width, peak
B1 amplitude and SAR with flexible trade-off among them.
Example designs for RF pulse in balanced SSFP C-13 MRI
and dualband saturation RF pulse for H-1 MR spectroscopy
are shown and validated.
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
Poster 201
Flip Angle Measurement for Quantitative Magnetic
Resonance Imaging
1, 2
1
4
Caroline Le Ster ; Giulio Gambarota ; Olivier Beuf ; Hervé
1, 3
Saint-Jalmes
1
2
Université de Rennes 1, LTSI, Rennes, France; Siemens
3
Healthcare, Saint Denis, France; Centre Eugène Marquis,
4
CRLCC, Rennes, France; CREATIS, Université de Lyon,
Villeurbanne, France
Quantitative MR methods often require the knowledge of the
local B1 field. Many B1 mapping methods have been
developed, but few of them are suited to measure low flip
angles. Here we use the Low Angle Method coupled with EPI
(LAM EPI) to acquire multislice B1 maps on a phantom and in
vivo on the brain and the abdomen (breathold acquisition). We
compare our results to the reference B1 mapping Double
Angle Method (DAM) and the classical LAM method (LAM
FLASH).
Poster 204
Estimates of Regional Brain Myelination Derived from
MRI with a New Bayesian Monte Carlo Approach
Mustapha Bouhrara; Richard G. Spencer
NIH, Baltimore, MD
Extraction of the myelin water fraction (MWF) from the
transverse decay signal relies upon the notoriously unreliable
process of inverting multiexponential decay data using least
squares-based algorithms. This leads to instability of
parameter estimates and redundancy between multiple
parameter sets that describe the decay signal equally well.
Therefore, we explored the use of Bayesian probability
analysis (BPA) for the estimation of MWF from mcDESPOT,
used extensively for MWF estimation, and compared the
results with those derived using the traditionally used
stochastic region contraction algorithm. Our BPA analysis
markedly improves accuracy and precision in the estimation of
MWF from two-component mcDESPOT signal model.
Poster 202
Gadolinium Nanocrystals with Large Magnetic Moments
for Applications in Biomolecular Imaging
Yavuz Ertas; Nanette Jarenwattananon; Louis-S. Bouchard
UCLA, Los Angeles, CA
We report the first successful production of solid core-shell
gadolinium
metal
nanocrystals.Chemical
synthetic
approaches fail to produce oxide-free nanoparticles due to the
aggressively reactive nature of lanthanides.We developed a
nanofabrication technique to overcome this problem which
resulted in the largest saturation magnetization observed to
date for nanocrystalline Gd.NMR relaxivity measurements
were performed to evaluate the performance of the
nanoparticles as potential MRI contrast agents.Typically,Gd
based nanoconstructs are T1 MRI contrast agents; however,
we demonstrate that Gd nanoparticles could be used as T2weighted agents.An unexpectedly high r2 of 232.06 mM.s^-1
per Gd atom has been obtained.A per-particle relaxivity of 3.6
× 10^8 mM.s^-1 has been achieved,which is the highest per
particle r2 relaxivity reported for any kind of T2 contrast
agents.
Poster 205
Reliable Detection of C2 and C4 Proton Signals in
Carnosine by MR Proton Spectroscopy
1
2
2
Kwan-Jin Jung ; Shahid Baba ; Aruni Bhatnagar ;
3
Susan Harkema
1
2
Radiology, University of Louisville, Louisville, KY; Medicine,
3
University of Louisville, Louisville, KY; KSCIRC, University of
Louisville, Louisville, KY
Carnosine (β-alanyl L-histidine) MR proton spectrum has two
peaks at 8 and 7 ppm from the C2 and C4 protons of the
imidazole ring. The C4 proton signal has been unreliable and
only the C2 proton signal has been used. This study is to
improve the detection of the C4 proton signal reliably by
suppressing the lipid signal at around 6 ppm adjacent to the
C4 proton signal. The reliable detection of both C2 and C4
proton signals allowed us to correlate the relative composition
of C2 and C4 protons to the long term usage of skeletal
muscles. In addition, the relative composition provided a selfcalibration feature which can simplify the application by
avoiding the difficult absolute quantification.
Poster 203
Optimal Glass Forming Solvent and Photo-Induced
129
Radicals bring Xe Hyperpolarization via SublimationDNP to Biomedical Imaging Standards
1
2
1
Andrea Capozzi ; Christophe Roussel ; Arnaud Comment ;
3
Jean-Noel Hyacinthe
1
Institute of Physics of Biological Systems, EPFL, Lausanne,
2
CH; Inst. of Chemical Sciences and Engineering, EPFL,
3
Lausanne, CH; School of Health Sciences, Geneva, CH
Despite unique biomedical applications from ventilation to
129
perfusion and molecular imaging, hyperpolarized (HP)
Xe
129
MRI suffers from the somehow limited availability of HP Xe.
129
Xe using a
Sublimation-DNP consists in producing HP
generic dissolution-DNP polarizer able to produce various HP
129
Xe and
tracers. It can contribute to a wider access to HP
spread of its unique applications. A limited polarization level
was precluding the potentially higher HP gas output. In the
present work we show how the combination of an optimal
glass-forming solvent with photo-induced radicals leads to
129
Xe polarization, and bring the technique to the
improved
biomedical imaging standards.
Poster 206
MR Proton Spectroscopy of Carnosine in Skeletal
Muscles of Individuals with Spinal Cord Injury
1
2
2
Kwan-Jin Jung ; Andrea Willhite ; Neesha Settipalle ; Maxwell
3
2
Boakye ; Susan Harkema
1
2
Radiology, University of Louisville, Louisville, KY; KSCIRC,
3
University of Louisville, Louisville, KY; Neurosurgery,
University of Louisville, Louisville, KY
Carnosine has been reported to be a biomarker of skeletal
muscle activity due to its antioxidant and anti-fatigue
properties. Therefore, it is our interest to study the carnosine
content in the skeletal muscles of complete SCI patients
before and after the treatment. The carnosine content in the
leg muscles of 5 participants was measured before the
treatment as a baseline using the MR proton spectroscopy at
3T MRI. The carnosine decreased markedly in the
gastrocnemius muscle than in the soleus muscle in the
complete SCI patients. Additionally, the carnosine in the two
muscles became equivalent with an increase in the post-injury
period.
Page 81
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
Poster 207
MR Volume Selective Spectroscopy of Carnosine Using
Phased Array RF Coil in Varian 9.4T MRI
Kwan-Jin Jung
Radiology, University of Louisville, Louisville, KY
A phased array receiving rf coil is preferred to a single loop rf
coil due to an increased sensitivity and the flexibility in
locating the voxel. Furthermore, the phased array rf coil does
not need an rf coil tuning due to its high impedance design
using a preamplifier. The Varian 9.4T MRI is equipped with
four parallel receiving channels, but it has not come with a
program to combine the spectra from multiple channels. A
simple and practical program is developed to combine the
multiple spectra into one spectra of carnosine. The phase shift
in each channel was estimated from a major spectral peak
(C4 proton). The estimated phase shift was corrected before
the summation of multiple spectra.
Poster 208
Covariance J-Resolved Spectroscopy (Cov-JPRESS) at
3T: Implementation and Pilot Feasibility
Zohaib Iqbal; M. Albert Thomas
UCLA, Los Angeles, CA
Localized
two-dimensional
J-Resolved
Spectroscopy
(JPRESS) is a powerful tool for discerning overlapping
metabolite resonances due to the increased spectral
dispersion from adding the second spectral dimension.
However, acquisition of this 2D data requires a significant
amount of time posing challenges with clinical validations. In
order to shorten acquisition time, a method utilizing
covariance NMR and post-processing is developed that only
samples a limited number of the total t1 points necessary for
JPRESS. These t1 points are used to create a covariance
matrix representative of the spectrum. GAMMA simulated
basis sets were used to find these optimized t1 combinations.
A qualitative analysis of retrospective phantom data using
these t1 combinations suggests possible accelerations of up
to three-fold for single-voxel JPRESS scans.
Poster 209
NMR Microscopy of Paraffin Embedded
Tissue In Mesophase
Istvan Pirko; Jeffrey D. Gamez; Prasanna K. Mishra;
Slobodan Macura
Mayo Foundation, Rochester, MN
Few degrees below the melting point paraffin exhibits the
mesophase behavior. In this state, the paraffin is solid enough
to preserve mechanical integrity of the formalin fixed paraffin
embedded (FFPE) block and soft enough to enable
embedded tissue imaging. The mesophase imaging will
enable truly noninvasive NMR imaging of FFPE tissue blocks.
This may be useful for reviewing the block content, like
noninvasive determination of tissue thickness within the block.
EXOTICA
210 - 228
Poster 210
A Fully Quantum Mechanical Theory of Radiation
Damping in NMR
James Tropp
GE Healthcare Technologies, Fremont, CA
Using methods borrowed from quantum optics, we obtain a
fully quantum-mechanical description of radiation damping in
Page 82
NMR, including the calculation, from first principles, of the of
signal power--including the enhancement of coherent
spontaneous emission by cavity coupling and stimulated
emission. Examples are also given of Rabi oscillation, and the
build-up of signal coherence in the probe.
Poster 211
Mo132 Meets Amino Acids and Peptides
1
1
1
Erhard T.K. Haupt ; Olga A. Petina ; Conrad Stork ;
2
2
Somenath Garai ; Achim Müller
1
Department Chemistry University Hamburg, Hamburg,
2
Germany; Department Chemistry, University Bielefeld,
Bielefeld, FRG
Mo132 (organic ligand) is a spherical, porous, nanosized
polyoxometallate-molecule with multiple interactions with its
environment, e.g.type of solvent, pH, temperature, or
chemical compounds in the solution. Of particular interest are
interactions with biologically relevant substances like amino
acids or peptides. Starting from single amino acids, the
behaviour of a peptide mixture is investigated as well as
interactions with a biologically active peptide hormone. A
possible application as an assignment aid in protein nmr is
discussed.
Poster 212
Frequency-Switched Off-Resonance Excitation
Carl A. Michal
University of British Columbia, Vancouver, Canada
A new strategy for radio-frequency excitation in magnetic
resonance experiments is introduced. The scheme is based
upon rf pulses that jump coherently back and forth between
frequencies that are offset far above and far below the
resonance(s) of interest. In the most straightforward
implementation, full-intensity NMR signals can be excited over
a bandwidth comparable to that of on-resonance rf of the
same rf power, but with the excitation at frequencies
arbitrarily far from resonance. With a careful choice of
parameters, the excitation bandwidth can be extended to
approximately three times that found for the same rf fieldstrength applied on-resonance. Other parameter regimes
promise to allow low-power narrow-band excitation,
simultaneous excitation and signal reception, and significant
sensitivity enhancements in wide-line spectroscopy.
Poster 213
Experimental Observation of a Phase Transition of the
Evolution of Many-Body Systems with
Dipolar Interactions
1
2
3
Gonzalo Agustin Alvarez ; Dieter Suter ; Robin Kaiser
1
2
Weizmann Institute of Science, Rehovot, Israel; Universität
Dortmund, Dortmund, Germany;
3
Institut Non-Lineaire de Nice, CNRS, Valbonne, France
We report the experimental observation of a phase transition
of the quantum coherent dynamics of a 3D many-spin system
with dipolar interactions, and determine its critical exponents.
Using NMR on a solid-state system of spins at roomtemperature, we quench the interaction Hamiltonian to drive
the evolution of the system. The resulting dynamics of the
system coherence can be localized or extended, depending
on the quench strength. Applying a finite-time scaling analysis
to the observed time-evolution of the number of correlated
spins, we extract the critical exponents v=s~0.42 around the
phase transition separating a localized from a delocalized
dynamical-regime. These results show that NMR quantum
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
simulations can model the non-equilibrium dynamics of
complex many-body systems, such as 3D spin-networks with
dipolar-interactions.
Poster 214
NMR Spin Noise Spectroscopy at Milli-Kelvin
Temperatures
1
2
2
Maria Theresia Pöschko ; David Peat ; John Owers-Bradley ;
1
Norbert Müller
1
2
Johannes Kepler University, Linz, Austria; University of
Nottingham, Nottingham, UK
The amplitudes and line shapes of spin noise power spectra
depend mainly on the transverse relaxation rates, the tuning
offsets, and the radiation damping rates. The high magnitude
of magnetization achieved by very low temperatures or
hyperpolarization causes strong radiation damping and thus
can greatly enhance the observation of nuclear noise spectra.
We report first results of proton spin noise spectra obtained in
a static magnetic field of 2.45 T at 17.5 mK using a He-3
cryostat. These spin noise spectra enable us to monitor the
build-up polarization and very slow longitudinal relaxation
processes avoiding any interference by radio frequency
pulses.
Poster 215
Spin Noise and Radiation Damping: Echoes, Non-Linear
Effects and Optimizing the Acquisition of 2D Noise
Detected NMR Spectra
1
1
1
Victor Rodin ; Stephan Ginthör ; Maria Theresia Pöschko ;
1
1
1,
Matthias Bechmann ; Kousik Chandra ; Judith Schlagnitweit
2
3
4
4
; Vilko Smrecki ; Gaspard Huber ; Hervé Desvaux ;
1
Norbert Müller
1
2
Johannes Kepler University, Linz, Austria; Centre de RMN à
3
Très Hauts Champs, Univ. de Lyon, Lyon, France; Rudjer
4
Boskovic Institute, Zagreb, Croatia; IRAMIS CEA/Saclay,
Gif-sur-Yvette, France
Spin noise spectra allow us to study and exploit radiation
damping effects in unique ways without interference through
radio frequency pulses, for which present several new
instances: noise gradient echoes, interference between
radiation damping and weak static field gradients,
enhancement of weak signals for the determination of isotope
effects, deuterium spin noise spectra, and optimized spin
noise detected 2D NMR experiments. A new simulation
approach allows for the consistent theoretical description of
spin noise and radiation damping phenomena with multiple
spin species including effects caused by the pre-amplifier,
which are not predicted by the theory of McCoy and Ernst
established in 1989.
Poster 216
Probing Molecular Dynamics at the Nanoscale via an
Individual Paramagnetic Center
1
2
2
Tobias Staudacher ; Nicole Raatz ; Sebastien Pezzagna ;
2
3
4
Jan Meijer ; Friedemann Reinhard ; Carlos Meriles ;
1
Joerg Wrachtrup
1
2
University of Stuttgart, Stuttgart, Germany; University of
3
Leipzig, Leipzig, Germany; Technical University of Munich,
4
Munich, Germany; CUNY-City College of New York,
New York, NY
We introduce a protocol using individual paramagnetic
nitrogen vacancy (NV) centers in diamond to observe the time
evolution of 1H spins from organic molecules on the diamond
surface. The protocol records spatiotemporal correlations
among the interacting 1H spins, and thus is sensitive to the
local system dynamics via its impact on the nuclear spin
relaxation and interaction with the NV. We demonstrate this
notion by comparing the NV response for solid and liquid
samples, where we identify substantial differences that we
interpret in terms of an interplay between molecular tumbling
and self-diffusion rates. Our observations are in agreement
with a model where molecules in the fluid transition from static
to mobile within ~1.5 nm from the surface.
Poster 217
Developing High-Resolution Carbon-13 and Silicon-29
MRI of Solids in Sedimentary Rocks
1
1
2
2
Robert Blum ; Sean Barrett ; Yi-Qiao Song ; Ravinath Kausik
1
Yale University, New Haven, CT;
2
Schlumberger-Doll Research, Cambridge, MA
Mapping pore structure and flow properties of sedimentary
rock is directly relevant to current challenges in geophysics
like carbon sequestration and oil field exploration. Such
applications require detailed information about both structure
and composition of porous rocks, but most existing scanning
methods tend to gather only one type of information.
Multinuclear MRI is a potentially powerful probe of these
interesting systems, but barriers such as magnetic
susceptibility inhomogeneity limit conventional approaches.
Here, we present our progress towards high spatial resolution
13
29
imaging of C and Si in sedimentary rock using the recently
developed quadratic echo line-narrowing sequence (M. Frey,
et al. PNAS 109: 5190 (2012)).
Poster 218
Time-Dependent Diffusion Measurement Reveals
Structural Correlations and Permeability of
Porous Films in a Layered Geometry
1
2
2
Antonios Papaioannou ; Dmitry S. Novikov ; Els Fieremans ;
1, 3
Gregory S. Boutis
1
Graduate Center of The City University of NY, New York, NY;
2
New York University School of Medicine, New York, NY;
3
Brooklyn College of The City University of NY, Brooklyn, NY
Molecular diffusion restricted by structural complexity at the
mesoscopic scale is ubiquitous in both biomedicine and
porous media. It was recently shown that the time
dependence of the diffusion coefficient distinguishes between
the disorder universality classes, and can be used to quantify
the permeability of the restrictions.
Here we measure the time-dependent diffusion coefficient of
water restricted by parallel porous films using PFG NMR. In
the long time limit (200ms<t<7.5s) our results reveal that the
diffusion coefficient approaches its tortuosity limit in a power
law way, in agreement with the short range disorder in the
arrangement of the films. In addition, the permeability of the
films is determined and compared with the value expected
from geometrical considerations.
Poster 219
New Developments in Optically Pumped NMR of
Semiconductors
1
1
1
Zayd Ma ; Matthew Willmering ; Erika Sesti ;
1
Sophia E. Hayes
1
Washington Univeristy, St. Louis, MO
Optically pumped NMR of semiconductors (OPNMR) is a
scheme to reveal new insight in spin-dynamics. However,
Page 83
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
studies up to this point have largely been focused on
measuring the NMR signal intensity as a function of laser
excitation energy to try and understand how absorption, i.e.
the “pumped” conduction band state, effects the resultant
nuclear spin orientation.
Our lab has developed new hardware to monitor the
polarization of photoluminescence during optical pumping
experiments (optically-detected NMR or ODNMR), maintain
cryogenic temperatures indefinitely, and excite two nuclei
simultaneously (i.e. a two-channel probe).
We present our initial studies using ODNMR on GaAs
quantum wells and preliminary cross-polarization OPNMR
results on CdTe from our newly constructed 2-channel
cyrogenic probe.
Poster 220
Residual Dipolar Couplings in Zero-to-Ultra-Low-Field
Nuclear Magnetic Resonance
1, 2
2, 3
John W Blanchard ; Tobias F Sjolander ; Jonathan P
2, 3
2
2
King ; Micah P Ledbetter ; Emma H Levine ; Vikram S.
2, 3
1, 2
2, 3
Bajaj ; Dmitry Budker ; Alexander Pines
1
2
Helmholtz-Institut Mainz, Mainz, Germany; UC Berkeley,
3
Berkeley, CA; Lawrence Berkeley National Laboratory,
Berkeley, CA
Zero-to-ultra-low-field nuclear magnetic resonance (ZULFNMR) provides a new regime for the measurement of nuclear
spin-spin interactions free from effects of large magnetic
fields, such as truncation of terms that do not commute with
the
Zeeman
Hamiltonian.
We
report
ZULF-NMR
measurements of residual dipolar couplings in acetonitrile-213
C aligned in stretched polyvinyl acetate gels, representing
the first investigation of dipolar couplings as a perturbation on
the indirect spin-spin J-coupling in the absence of an applied
magnetic field. As a consequence of working at zero magnetic
field, we observe terms of the dipole-dipole coupling
Hamiltonian that are invisible in conventional high-field NMR.
Poster 221
Multipulse Double-Quantum Magnetometry with NearSurface Nitrogen-Vacancy Centers
1
1
1
1
H. J. Mamin ; M. H. Sherwood ; M. Kim ; C. T. Rettner ; K.
2
3
1
Ohno ; D. D. Awschalom ; D. Rugar
1
2
IBM Almaden Research Center, San Jose, CA; University of
3
California, Santa Barbara, CA; U. of Chicago, Chicago, IL
Nitrogen-vacancy (NV) centers in diamond are remarkable
quantum mechanical objects that can act as sensitive atomicscale magnetometers. In most NV magnetometry
experiments, a single microwave frequency is used to
manipulate two of its three triplet-state sublevels, though more
recent schemes take full advantage of the S=1 nature. Here
we develop theoretically and experimentally a dual frequency
microwave pulsing scheme[1] that is twice as sensitive to ac
magnetic fields as conventional two-level magnetometry.
Using multipulse sequences of up to 128 pulses under
optimized conditions, we show enhancement of the SNR by
up to a factor of 2 in detecting NMR statistical signals, with a
4× enhancement theoretically possible.
[1] H. J. Mamin et al, Phys. Rev Lett. 113, 030803 (2014).
Poster 222
Proton Magnetic Resonance Imaging with a NitrogenVacancy Spin Sensor
Page 84
1
1
1
Mark Sherwood ; John Mamin ; Moonhee Kim ; Charles
1
2
3
1
Rettner ; Kenichi Ohno ; David Awschalom ; Daniel Rugar
1
2
IBM Almaden Research Center, San Jose, California; UC
Santa Barbara, Santa Barbara, CA;
3
University of Chicago, Chicago, IL
The extension of MRI resolution to the nanometer scale would
provide a powerful new form of microscopy that could have
revolutionary impact on the nanosciences, especially
nanobiology where the ability to nondestructively image a
single macromolecular complex could be extremely useful.
The biggest challenge is to overcome the severe sensitivity
limitations of conventional inductive detection techniques. We
1
H MRI at room
demonstrate two-dimensional (2D)
temperature on a nanometer scale organic polymer test
sample using a single NV center in diamond as the sensor.
The sample–diamond contact is scanned past the NV sensor
in order to build up a two dimensional image. A spatial
resolution of approximately 12 nm is demonstrated, limited
primarily by the scan resolution.
Poster 223
Electrochemical Enhancement of Sensitivity in NMR
Ping He; Jamie Walls
Department of Chemistry, Coral Gables, FL
NMR's low sensitivity places severe constraints on the types
of problems/amount of sample that can be reasonably
detected. Methods to improve sensitivity have mainly focused
on increasing the S/N, and very little work has been
performed on decreasing the time between acquisitions,
which is determined by T1. In this work, we propose to
improve sensitivity by reducing the time between acquisitions
using electrochemical techniques. A three electrode
electrochemical cell (EC) insert for use in a 5mm NMR tube
was built. Voltage pulses applied between acquisitions were
used to generate and to remove paramagnetic species in
order to artificially reduce T1. Preliminary results indicate an
enhancement of 40-50% for the long-relaxing CHD2CN
resonance in a ferrocene/acetonitrile solution.
Poster 224
Nuclear Spin Diffusion in a Quasi-1D Crystal
1
2
2
Steven W. Morgan ; Xuan Wei ; Paola Cappellaro ;
1
Gregory S. Boutis
1
Brooklyn College of CUNY, Brooklyn, NY;
2
MIT, Cambridge, MA
Spin diffusion is the process whereby nuclear spin
magnetization (or energy) is transported by energy conserving
flip-flop interactions. Spin diffusion of Zeeman and interspin
energy have been previously measured by NMR scattering
methods. We report measurements of Zeeman spin diffusion
in a single crystal of fluorapatite along the c axis. When the
magnetic field is oriented along this axis of the crystal the
contributions from the nearest neighbors along the spin chain
account for 97% of the total second moment. Preliminary data
indicate that the Zeeman spin diffusion coefficient is faster
than has been measured in calcium fluoride.
Poster 225
T2-D Studies of Biomolecular Interactions Using Singlesided NMR
Tyler Meldrum; John Gray
The College of William & Mary, Williamsburg, VA
We have employed two-dimensional T2-D relaxometry with a
single-sided magnet to probe changes in molecular size
POSTERS
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
during the titration of the ligand naproxen with its ligand host
protein bovine serum albumin (BSA). We are able to see
changes in T2-D signals with changing concentrations,
demonstrating the use of single-sided hardware in monitoring
biomolecular interactions.
Poster 226
Cross-Relaxation Spectroscopy using Nitrogen-Vacancy
Centers in Diamond
1, 2
1, 2
1
Claudia Avalos ; Hai-Jing Wang ; Julian Schwartz ; Chang
1, 2
1, 2
1, 2
1, 2
Shin ; Scott Seltzer ; Vikram Bajaj ; Alexander Pines
1
2
Lawrence Berkeley National Lab, Berkeley, CA; University of
California - Berkeley, Berkeley, CA
The application of magnetic resonance spectroscopy at
progressively smaller length scales may eventually permit
‘chemical imaging’ of spins at the surfaces of materials and
biological complexes. In particular, the negatively charged
nitrogen-vacancy (NV−) centre in diamond has been exploited
as an optical transducer for nanoscale nuclear magnetic
resonance. However, the spectra of detected spins are
generally broadened by their interaction with proximate
paramagnetic NV− centers through coherent and incoherent
mechanisms. Here we make progress towards using optically
detected cross relaxation to resolve the spectra of electron
spins coupled to NV− centers external to the diamond lattice.
Using an ensemble of NV- centers <8 nm from the diamond
surface we probe the chemical structure of 2,2-diphenyl-1picrylhydrazyl at a earth's magnetic field.
Poster 227
Advances in Pulsed Zero Field NMR
1
1, 2
3
Tobias Sjolander ; Michael Tayler ; John Blanchard ;
1, 4
1, 3
1, 4
Jonathan P King ; Dmitry Budker ; Alex Pines
1
2
UC Berkeley, Berkeley, California; University of Cambridge,
3
Cambridge, UK; Helmholz Institut, Mainz, Mainz, Germany;
4
Lawrence Berkeley National Lab,
Berkeley, CA
This presentation concerns Zero and Ultra-Low-Field NMR
and I will present some of our recent work in developing and
implementing new pulsed methods for use in the Zero-Field
regime. Using weak, resonant magnetic fields we are able to
drive transitions directly between the Zero-Field eigenstates
as opposed to the hard spin rotations by DC pulses used to
date. Further, by using orthogonal coils to generate rotating
fields we are able to side step the Fourier limit on frequency
selectivity. We have also performed a near zero field
heteronuclear decoupling experiment, taking a carbon
decoupled proton spectrum in a regime where the scalar
coupling is several times larger than the Zeeman interaction
with an applied field.
Poster 228
Decoherence-Protected Spin Transitions of Nitrogen
Vacancy Centers in 99% Carbon-13 Diamond
1
1
1
3
Anna Parker ; Haijing Wang ; Yiran Li ; Dmitry Budker ;
2
2
Alex Pines ; Jonathan P King
1
2
Universiy of California, Berkeley, Berkeley, CA; UC
3
Berkeley, Berkeley, CA; UCB Physics, NSD LBNL,
Berkeley, CA
Nitrogen vacancy (NV ) centers in diamond are a prime
candidate for use in quantum information devices, owing to
their spin-1 ground state, straightforward optical initialization
and readout, and long intrinsic coherence times in a roomtemperature solid. In this study, we investigate an ensemble
13
of NV centers in 99% C diamond by optically-detected
magnetic resonance (ODMR). While the pure electron spin
transitions of this system are broadened by interactions with
13
the C spin bath, Zero First Order Zeeman term (ZEFOZ)
transitions that are desensitized from fluctuating magnetic
fields exist at certain magnetic fields. By observing transitions
near these points, inhomogeneous linewidths are narrowed by
factors as high as 130. These transitions may be used to store
quantum information in long-lived coherences.
HYPERPOLARIZATION AND DNP
229 - 275
Poster 229
Analyzing Synthetic Polymers by Dynamic Nuclear
Polarization Solid-State Nuclear Magnetic Resonance
1
1
1
2
Dao Le ; Olivier Ouari ; Trang Phan ; Fabio Ziarelli ; Fabien
3
1
1
1
Aussenac ; Gilles Casano ; Pierre Thureau ; Didier Gigmes ;
1
1
Paul Tordo ; Stéphane Viel
1
Aix-Marseille Univ. & CNRS, ICR UMR 7273, Marseille,
2
France; Aix-Marseille Univ, Centrale Marseille, CNRS,
3
Marseille, France; Bruker Biospin SAS,
Wissembourg, France
This communication describes our ongoing efforts in using
high-field Dynamic Nuclear Polarization (DNP) for the
characterization of polymers by solid-state NMR. All together,
we show that the large sensitivity enhancements provided by
DNP (here between 10 and 40) allows for the structural
elucidation of chain-ends of functional polymers of relatively
high molecular weight. This unprecedented sensitivity
improvement opens up new avenues for the characterization
of synthetic polymers, and paves the way to a finer description
of the fundamental microstructure/morphology/properties
relationships in polymeric materials.
Poster 230
129
Long Storage Times for Hyperpolarized Xe and Precise
Measurement of its Absolute Polarization
1
2
1
Maricel Repetto ; Earl Babcock ; Peter Bluemler ; Werner
1
1
1
1
Heil ; Sergei Karpuk ; Kathlynne Tullney ; Stefan Zimmer
1
2
Institute of Physics, Mainz, Germany; Forschungszentrum
Jülich, Outstation at MLZ, Garching, Germany
All applications of hyperpolarized (HP) Xenon profit from high
polarization degrees (PXe) and long storage times for
preserving it. PXe is usually determined via comparison of the
NMR signals from HP-Xe with that of a thermally polarized
1
sample (typically H2O or Xe) involving many experimental
uncertainties. A simple, accurate and inexpensive method
was developed to determine PXe by directly measuring its
macroscopic magnetization.
The storage times for HP Xe with different buffer gases were
measured in rubidium-free, bare glass cells of GE180. The
wall relaxations obtained were around 16h with a high
reproducibility and finding the highest destruction rate for Xedimers for CO2 as a buffer gas. In addition, a strong
dependence on the isotopic abundance of Xe was identified.
Poster 231
Ultrafast Multidimensional Laplace NMR
1
1
2
Ville-Veikko Telkki ; Susanna Ahola ; Vladimir Zhivonitko ;
1
Otto Mankinen
1
2
University of Oulu, Oulu, Finland; International Tomography
Center SB RAS, Novosibirsk, Russia
Page 85
POSTERS
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
Laplace NMR (LNMR), i.e., relaxation and diffusion NMR
experiments, provide versatile information about the dynamics
and structure of substances. Like in traditional NMR
spectroscopy, the resolution and information content of LNMR
can be increased by a multidimensional approach. However,
long experiment time restricts the applicability of the
multidimensional methods. As a solution for this problem, we
are developing a broad range of ultrafast, single-scan
multidimensional LNMR experiments, based on the principles
of continuous spatial encoding that have been recently
successfully applied in ultrafast multidimensional NMR
spectroscopy. The method shortens the experimental time by
one to three orders of magnitude, offering unprecedented
opportunities to study fast processes in real-time as well as to
utilize the significant sensitivity gain of hyperpolarized
substances.
Poster 232
Production of Hyperpolarized Liquids under Continuous
Flow Conditions
1
1
1
Kerstin Münnemann ; Manuel Braun ; Barbara Piechalska ;
2
2
2
Benjamin Niederländer ; Maricel Repetto ; Peter Bluemler ;
2
Werner Heil
1
Max Planck Institute for Polymer Research, Mainz, Germany;
2
Institute of Physics, Mainz, Germany
Production of hyperpolarized liquids in a continuous flow
mode using two different polarization methods (spin exchange
129
Xe and PHIP) are demonstrated. In
optical pumping for
order to dissolve HP-Xe and parahydrogen for the
homogeneous hydrogenation reaction in a PASADENA
experiment (chemical reaction inside the spectrometer) hollow
fiber membranes were used. Using this membrane technique,
hydrogen, which otherwise is only poorly soluble, can be
dissolved efficiently in the aqueous reaction mixture. This
provides the opportunity to accelerate the reaction and to
bring parahydrogen molecularly into the solution without the
problem of foaming and bubbles. Due to this gentle
hydrogenation conditions it is possible to measure a
PASADENA spectrum under continuous flow with a brilliant
spectral resolution.
Poster 233
Optical Alignment of Spins: OPNMR Signal Dependence
on Excitation Energy in GaAs QWell and Bulk CdTe
Matthew M. Willmering; Zayd L. Ma; Erika L. Sesti;
Sophia E. Hayes
Washington University in STL, St. Louis, MO
Optically Pumped NMR (OPNMR) of semiconductors is an
established technique that transfers angular momentum from
spin polarized conduction electrons to surrounding nuclei. We
present OPNMR profiles on two separate groups of
semiconductor samples. Group 1 consisted of bulk CdTe
samples with different resistivities, crystallinities, and an
addition of a dopant (Zn). Differences in the OPNMR profiles
of bulk CdTe samples with varying physical characteristics are
observed and will be shown. The other sample group was a
pair of identical GaAs quantum wells with a thickness of 16.9
nm. Measurements of the light hole to conduction band
transition energy studied as a function of magnetic field using
OPNMR will also be shown.
Page 86
Poster 234
Detecting Nanodiamonds with DNP
1, 2
1, 3
3,
David Waddington ; Mathieu Sarracanie ; Huiliang Zhang
4
2
3, 4
1, 3
; David Reilly ; Ronald Walsworth ; Matthew Rosen
1
MGH/A.A. Martinos Center for Biomedical Imaging,
2
Charlestown, MA; School of Physics, University of Sydney,
3
Sydney, Australia; Department of Physics, Harvard
4
University, Cambridge, MA; Harvard-Smithsonian Center for
Astrophysics, Cambridge, MA
This work aims to develop a new bio-probe based on the
detection and tracking of nontoxic nanoparticles in biological
environments. We report the first DNP enhancement of 1H in
a nanodiamond/water solution at very low magnetic field.
Overhauser-enhanced MRI (OMRI) utilizes the nuclear
hyperpolarization of hydrogen to detect paramagnetic species.
A –1.36 times enhancement of the 1H signal has been
demonstrated in a 10%/wt solution of 100 nm natural
nanodiamonds (Microdiamant) and DI water at 6.5 mT. This
result will drive further research into the use of OMRI
methodologies as a means of tracking nanoparticles in vivo.
Poster 235
New Approaches for Production and Application of
Parahydrogen-Induced Polarization (PHIP) in
Heterogeneous Hydrogenations
1, 2
1
1, 2
Oleg Salnikov ; Kirill Kovtunov ; Danila Barskiy ;
3
1, 2
Eduard Chekmenev ; Igor Koptyug
1
2
ITC, SB RAS, Novosibirsk, Russian Federation; Novosibirsk
3
State University, Novosibirsk, Russian Federation; Vanderbilt
University Institute of Imaging Science, Nashville, TN
Parahydrogen-Induced Polarization (PHIP) is a useful
technique providing significant enhancement of NMR signal.
Moreover, PHIP can be used for mechanistic studies of
catalytic reactions.
In this work it was shown that gas-liquid biphasic
hydrogenation with parahydrogen can be used for production
of catalyst-free hyperpolarized gases. It was demonstrated
that PHIP effects can be observed in heterogeneous
hydrogenations over bulk metals and metal oxides. PHIP was
used
for
mechanistic
studies
of
heterogeneous
hydrogenations. The existence of route of pairwise hydrogen
addition to C=C bonds of acrolein, crotonaldehyde and vinyl
acetate was demonstrated. In hydrogenation of acrolein and
vinyl acetate over Rh catalysts the formation of hyperpolarized
2-butene was observed. In propene-d6 hydrogenation the
H/D-exchange via hydrogen addition with subsequent
dehydrogenation was demonstrated.
Poster 236
Producing and Revealing Hyperpolarization in Equivalent
Spin Pairs Supporting Long-Lived States (HELLS)
1
1
1
Aurélien Bornet ; Xiao Ji ; Daniele Mammoli ; Basile
1
1, 2
1
Vuichoud ; Geoffrey Bodenhausen ; Jonas Milani ;
1, 3
Sami Jannin
1
2
EPFL, Lausanne, Switzerland; Ecole Normale Supérieure,
3
Paris, France; Bruker BioSpin AG, Fallanden, Switzerland
Hyperpolarization lifetimes are usually limited to nuclear spinlattice relaxation times. These lifetimes can sometimes be
extended by storing the hyperpolarization in the form of longlived states (LLS) that are immune to most dominant
relaxation mechanisms.
POSTERS
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
We show here how LLS can be readily populated by
dissolution DNP (d-DNP) in molecules that contain two
magnetically equivalent spins in solution. Alike para-hydrogen,
HELLS are sustainable over long timescales, and are not
magnetically active. However, they can be revealed by
breaking symmetry, for example by an enzymatic process
such as the conversion of fumarate HELLS into malate.
We are currently investigation the applicability of HELLS to a
wider family of molecules containing magnetically equivalent
pairs of spins, such as CH2RR’, CH2Cl2, or H2O.
Poster 237
Measuring Singlet State Lifetimes in Nearly Equivalent
Systems using PHIP
Yuning Zhang
New York University, New York, NY
Hyperpolarization and singlet state NMR can be used to
overcome the shortcomings of low sensitivity and short
lifetime. Nearly equivalent molecules hyperpolarized by parahydrogen induced polarization (PHIP) are direct sources of
such long-lived singlet order. To reveal this silent singlet state,
Spin Lock Induced Crossing was successfully used recently.
Here, we present that PHIP originated singlet state in a
homonuclear 4-spin system can be revealed by weak power
spin-lock as well. Much longer duration of spin-lock is required
and the transfer efficiency is low. Consequently, the lifetimes
can only be measured using hyperpolarized samples. We
show that lifetimes and efficiencies can be extracted by using
PHIP and a multi-conversion method. This method is used to
measure lifetimes in water-diluted solvents.
Poster 238
New Biosensing Strategies Using Hyperpolarized Xenon129 NMR Spectroscopy
Yanfei Wang
University of Pennsylvania, Philadelphia, PA
Hyperpolarized 129Xe chemical exchange saturation transfer
(Hyper-CEST) biosensors are a novel class of NMR/MRI
contrast agents with high sensitivity, and as such have great
potential to image molecular targets at low abundance that
cannot be investigated by conventional proton MRI.
Cryptophane-A and its derivatives are the most studied Xebinding cages, and several cryptophane-based 129Xe
biosensors have been used for different detection purposes.
However, synthetic challenges have limited broad usage of
cryptophane biosensors. Here, we show that commercially
available cucurbit[6]uril is a novel Hyper-CEST NMR contrast
agent, detectable at 1.8 picomolar concentration at 300 K with
rapid xenon exchange kinetics. This allows for sensitive
detection of biologically important analytes such as
polyamines.
Poster 239
In vivo Temperature Imaging using Lipid-dissolved
Hyperpolarized Xenon-129
Alex Burant; Le Zhang; Drew McCallister;
Rosa Tamara Branca
University of North Carolina at Chapel Hill, Chapel Hill, NC
Noninvasive, in vivo temperature measurements of fatty tissue
have proven to be quite difficult. Advances in hybrid PRF/T1
based measurements have allowed for improvements in
accuracy but are still not ideal for fatty tissues like brown
adipose tissue. We demonstrate a method to obtain in vivo
temperature maps of fatty tissue using hyperpolarized xenon129. Brown adipose tissue (BAT) is a fatty tissue which
produces heat during metabolic stimulation by transforming its
internal fat into heat. As the hydration of BAT changes during
this process, PRF/T1 based measurements cannot accurately
determine temperature changes. Xenon is highly lipophilic and
the lipid-dissolved xenon frequency is strongly temperature
dependent, allowing for the production of accurate relative
temperature maps.
Poster 240
129
A Sensitive Hg(II)-Activated Xe NMR
Molecular Clamp Biosensor
Qianni Guo; Qingbin Zeng; Weiping Jiang; Qing Luo;
Xin Zhou
Wuhan Inst. of Physics and Mathematics, CAS,
Wuhan, Hubei, China
Mercury contamination is widespread and arises from a
variety of natural sources.We propose the use of
129
Xe nuclear magnetic resonance (NMR)
hyperpolarized
2+
spectroscopy for the sensitive detection of Hg ions in
aqueous solution.We develop a biosensor whose molecular
2+
structure is like a clamp. When interact with Hg , the
molecular structure of the biosensor could be changed as a
clamp from “open” to “closed”. This molecular structure
change causes the distance between the two cryptophane
cages become closer, and the electron cloud of them
overlapped. As a result, comparing with normal downfield
chemical shifts of the reported xenon biosensors formetallic
ions, the Xe caged in the cryptophane moiety shows a upfield
chemical shift change from 66.5 ppm to 66.1 ppm.
Poster 241
H NMR Relaxation Analysis of UV-cured Acrylate
Hydrogel Network
Bing Wu; Dermot Brougham
Dublin City University, Dublin, Ireland
Due to its biocompatibility, PEG-based hydrogel has been
widely used in tissue engineering and coating applications.
Meanwhile, photocuring among all the curing procedures,
offers great advantages (e.g. the ease of applicability) for
preparing crosslinked polymer. Hence, a thorough
understanding of the network topology of these photo-cured
PEG-based acrylate hydrogels hold great interests in the
industrial application of this material, since the topological
properties are crucial in rubber elasticity of the hydrogel. In
this study, a new NMR approach was designed to analyze the
topological heterogeneity of the acrylate hydrogel sample
through a combination of Hahn-Echo Pulse-sequence (HEPS)
and MQ NMR analysis. And the results also have been
discussed with the corresponding chromatographic data.
1
Poster 242
Ultra-narrow Line Diode Laser Systems for Optical
Pumping of K, Rb, Cs, and Ar Gases
Aleksandr Ryasnyanskiy; Lawrence Chase; Travis Wood;
Vadim Smirnov; Oleksiy Mokhun; Alexei Glebov; Leonid
Glebov
OptiGrate Corp., Orlando, FL
We present the results of the development of narrowband (15100 pm) laser diode systems operating at variety of
wavelengths and covering different application areas: Spin
exchange optical pumping (770 nm for potassium, 794.7 for
rubidium), Diode pumped alkali lasers (780 nm – rubidium,
Page 87
POSTERS
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
852 nm – cesium), Raman spectroscopy (785 nm), and
pumping of rare gas (Argon) metastable laser (811 nm).
Poster 243
Improving SABRE to Hyperpolarize and Image Nitrogen15 in Biomolecules
1
1
3
Thomas Theis ; Warren S. Warren ; Fan Shi ; Boyd M.
3
2
2
2
Goodson ; Milton Truong ; Aaron Coffey ; Roman Shchepin ;
2
Eduard Chekmenev
1
2
Duke University, Durham, NC; Vanderbilt University Institute
3
of Imaging Science, Nashville, TN; Southern Illinois
University, Carbondale, IL
Two improvements to SABRE, based on new quantum
mechanical insights into the heteronuclear SABRE process,
produce unprecedented 15N-hyperpolarization levels (up to
10%). SABRE-SHEATH uses μT-fields established by
magnetically shielding the Earth’s field; LIGHT-SABRE
enables efficient in magnet hyperpolarization at any field
strength, thus eliminating the requirement for sample transfer
from a distinct hyperpolarizing region. Hyperpolarization is
demonstrated on 15N-pyridine and 15N-nicotinamide, and we
believe that the presented 15N-SABRE schemes will work for
all molecules that have successfully been hyperpolarized with
traditional 1H-SABRE. With the hyperpolarized 15N-signals
we have acquired what we believe is the first 15N-image.
These results strongly suggest that inexpensive, highly
efficient hyperpolarization (and even continuous in-magnet
hyperpolarization) is possible.
Poster 244
Biomolecular DNP- supported NMR Spectroscopy using
Site-Directed Spin Labelling
1
1
2
Elwin Van der Cruijsen ; Eline Koers ; Claire Sauvee ; Deni
1
1
2
2
Mance ; Markus Weingarth ; Olivier Ouari ; Paul Tordo ;
1
Marc Baldus
1
2
Utrecht University, Utrecht, Netherlands; Aix-Marseille
Université, Marseille, France
Site-directed spin labeling is a powerful approach to exploit
local PRE-effects in NMR-based Structural biology. We
investigate whether DNP can be established by creating local
spin clusters via site-directed spin labeling. We examined how
site-directed spin labelling modulates structural and dynamical
properties of the target protein of interest. Subsequently, we
determined DNP enhancements as a function of the degree of
paramagnetic labeling and the spin label location at 400 and
800 MHz DNP conditions. In parallel, we conducted quantummechanical
model
calculations
that
predict
DNP
enhancements on the basis of the spin cluster size. Taken
together, our results suggest that the creation of local spin
clusters can generate sizable DNP enhancements while
preserving the intrinsic benefits of PRE-based NMR
approaches.
Poster 245
Enhancing and Predicting the Electron-Nuclear Scalar
and Dipolar Interaction in Liquid State Dynamic Nuclear
Polarization
2
1
2
2
Xiaoling Wang ; William Isley ; Sandra I. Salido ; Ziqi Sun ;
1
2
Christopher J. Cramer ; Harry C. Dorn
1
Department of Chemistry, University of Minnesota,
2
Minneapolis, MN; Department of Chemistry, Virginia Tech,
Blacksburg, VA
In the current study, we demonstrate that solutes dissolved in
supercritical fluid CO2, for low to high field flow transfer DNP
Page 88
approaches result in enhanced dipolar interactions and exhibit
significant OE DNP enhancements at higher magnetic fields
as a result of reduced correlation times. For the case of the
13C NMR nuclide, significant scalar interactions and
corresponding large positive enhancements are obtained at
high magnetic fields for cases where weak hydrogen bonding
interactions are present in the nitroxide-substrate complex.
We directly compare intermolecular scalar hyperfine couplings
with experimental scalar DNP data utilizing density functional
theory (DFT) computational approaches. This provides direct
predictions in a given scalar interaction dominated radicalsubstrate system of the DNP enhancement for the first time in
literature.
Poster 246
Parahydrogen Induced Hyperpolarization of Long-Lived
Spin States of Propanes for Gas Imaging
1
2
1
Kirill Kovtunov ; Milton Truong ; Danila Barkiy ; Oleg
1
2
2
1
Salnikov ; Aaron Coffey ; Kevin Waddell ; Igor Koptyug ;
2
Eduard Y Chekmenev
1
International Tomography Center (ITC), Novosibirsk, Russia;
2
Vanderbilt University Institute of Imaging Science,
Nashville, TN
Long-lived spin states (LLSS) of propane gas are induced by
parahydrogen at low magnetic field in the J-coupling
dominating regime. As a result, LLSS can preserve the
produced proton hyperpolarization significantly longer with
TLLSS ~ 4.7 s for non-deuterated propane and TLLSS ~ 4.7 s for
propane-d6. As a result, high-resolution MRI of stopped
hyperpolarized (%PH~1%) propane gas is feasible over a time
window of > 10 s, which is now sufficient for prospective in
vivo administration by gas inhalation, potentially providing an
advantageous (production scale and cost, and the use of
convectional
proton
MRI
scanner)
alternative
to
129
Xe. The use of low-field MRI for propane
hyperpolarized
imaging carries multiple additional advantages related to
background signal, detection sensitivity and others.
Poster 247
Open-source Automation of PHIP and SEOP
Hyperpolarizers
1
1
1
Aaron Coffey ; Roman Shchepin ; Milton Truong ; Wellington
1
2
3
Pham ; Boyd M. Goodson ; Michael J. Barlow ; Matthew
4
1
1
Rosen ; Kevin Waddell ; Eduard Chekmenev
1
2
Vanderbilt University (VUIIS), Nashville, TN; Southern
3
Illinois University, Carbondale, IL; University of Nottingham,
4
Nottingham, UK; MGH/A.A. Martinos Center, Boston, MA
Biomedical hyperpolarizers involve many complex steps
significantly benefiting from device automation. In this work,
an open-source software and hardware approach was
developed for PHIP and SEOP hyperpolarizers producing
agents for in vivo preclinical and clinical use. The key
advantages are robustness (i.e. the microcontroller
seamlessly integrates control of solenoid and pneumatic
valves, the NMR spectrometer, power supplies and other
components of SEOP and PHIP hyperpolarizers) and low
cost. In particular, an open-source PHIP hyperpolarizer design
13
will be presented capable of >15% C polarization for the
only two metabolic contrast agents (succinate and
phospholactate) showing promise in vivo to date. The opensource PHIP hyperpolarizer (with in situ QA) produces HP
13
13
C-phospholactate enabling whole-body C lactate MRS
following tail-vein HP phospholactate injection.
POSTERS
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
Poster 248
Spiral-based Compressed Sensing for Accelerated
13
Hyperpolarized C MRSI
1
2
1
1
Peter Shin ; Michael Lustig ; Zihan Zhu ; Andrei Goga ;
1
Daniel Vigneron
1
2
UCSF, San Francisco, California; UC Berkeley,
Berkeley, CA
13
In hyperpolarized C experiments, data acquisition window is
limited by the rapid metabolism and T1 relaxation of the
hyperpolarized signal. Hence, we developed and evaluated
the performance of an accelerated acquisition and
13
C MR
reconstruction method for hyperpolarized
spectroscopic imaging (MRSI). More specifically, an
undersampled, spiral-based pulse sequence and an
accompanying compressed sensing reconstruction was
developed. Finally, we applied the developed technique to in
13
vivo [1- C]pyruvate imaging of breast cancer mice.
Poster 249
13
Robust Level Anti-Crossing Induced C
Hyperpolarization in 10% Enriched Diamond Crystals
1
1
Christian Oliver Bretschneider ; Gonzalo Augustin Alvarez ;
2
2
2
1
Ran Fischer ; Paz London ; David Gershoni ; Lucio Frydman
1
2
Weizmann Institute, Rehovot, Israel; Technion,
Institute of Technology, Haifa, Israel
Nitrogen-vacancy (NV) centers in diamond have numerous
intriguing properties making them a very interesting system to
investigate single-spin and ensemble phenomenons.
Common electron → nucleus polarization techniques facilitate
excited-state level anti-crossings (ESLAC) of energy levels.
This energy matching condition requires a careful positioning
of the diamond lattice with respect to the magnitude and
orientation of an external magnetic field. Deviations from that
optimal condition as much as 1 degree result in a severe loss
of nuclear hyperpolariztion. In this study we show that a
13
modest enrichment of the C species (10%) broadens this
matching condition by at least one order of magnitude
increasing the scope of application for this interesting
hyperpolarization technique.
Poster 250
C in Diamond Powders be Polarized in Single-Digit
Gauss Fields?
1
1
Christian Oliver Bretschneider ; Gonzalo Augustin Alvarez ;
2
2
2
1
Ran Fischer ; Paz London ; David Gershoni ; Lucio Frydman
1
2
Weizmann Institute, Rehovot, Israel; Technion, Institute of
Technology, Haifa, Israel
Nitrogen-vacancy (NV) color centers in diamond exhibit many
intriguing properties, making them interesting candidates for a
wide range of physical applications. NV-C13 polarization
transfer techniques are restricted to single-crystals, however,
polycrystaline powders have more favorable properties for
potential polarization transfers outside the diamond lattice.
One possible approach is the use of very low magnetic fields
which would render all different crystallographic orientations
identical. We have developed a μwave-assisted roomtemperature hyperpolarization technique that exploits the
asymmetries in the electron-nucleus energy level manifolds.
In this study we show that the use of circularly polarized
radiation fields generates a macroscopic 13C polarization
even in single-digit Gauss fields. As a result, the proposed
polarization transfer scheme might also be suitable for
diamond powders.
Can
13
Poster 251
Photo-Induced Non-Persistent Radicals as Polarizing
Agents for Multi-Nuclei Dissolution-DNP
1
2
3
Andrea Capozzi ; Jean-Noël Hyacinthe ; Tian Cheng ; Tim
1
4
5
Eichhorn ; Giovanni Boero ; Christophe Roussel ;
1
Arnaud Comment
1
Institute of Physics of Biological Systems, EPFL, Lausanne,
2
Switzerland; School of Health Sciences, Geneva,
3
Switzerland; Laboratory for Biological Geochemistry, EPFL,
4
Lausanne, Switzerland; Laboratory of Microsystems 1, EPFL,
5
Lausanne, Switzerland; EPFL, Lausanne, Switzerland
The spin polarization of long-T1 nuclear isotopes in molecules
incorporated into radical-doped frozen amorphous solid
samples can be enhanced by dynamic nuclear polarization
(DNP) at low temperature and moderate magnetic field and
maintained through a rapid dissolution procedure to obtain
liquid-state hyperpolarized solutions. It has been recently
shown that non-persistent radicals useful for DNP can be
produced, by means of UV irradiation of pyruvic acid (PA)
frozen pellets. We demonstrate here how the radical induced
13
on the PA is able not only to polarize C nuclei on the
molecule itself, but also carbon nuclei on other chemical
129
Xe nuclei. It is moreover shown that the
species and
deuterated form of PA shows better DNP performances since
its sharper EPR line.
Poster 252
Shape-Dependent Parahydrogen Induced Polarization on
CeO 2 Nanoparticles
1
2
1, 3
2
Evan Zhao ; Haibin Zheng ; Ronghui Zhou ; Wei Cheng ;
2
1
Helena Hagelin-Weaver ; Clifford R Bowers
1
2
Chemistry, University of Florida, Gainesville, FL; Chemical
3
Engineering, University of Florida, Gainesville, FL; ColgatePalmolive Technology Center, Piscataway, NJ
We demonstrate the facet effect of nanoparticles on the signal
enhancement of parahydrogen induced polarization through
controlled synthesis of CeO2 nanooctahedra and nanorods.
The facet-dependence of the pairwise hydrogenation reaction
is revealed, thanks to the underlying mechanism of PHIP. Our
results show that the PHIP signal enhancement, and thus the
pairwise selectivity of dihydrogen addition, is higher in the
nanooctahedra than in the nanorods. This is attributed to the
different atomic configurations on the surface of different
facets.
Poster 253
Electron-Nuclear Cross Polarization: A Pulsed DNP Study
1, 2
2
2
Thach Can ; Joseph Walish ; Timothy Swager ;
1, 2
Robert Griffin
1
2
Francis Bitter Magnet Lab, Cambridge, MA; Department of
Chemistry, Mass. Inst. of Tech., Cambridge, MA
We performed electron rotating frame - proton lab frame cross
polarization, a time domain DNP experiment, at 0.35 T using
Nuclear Orientation Via Electron Spin Locking (NOVEL)
sequence on a series of samples including a single crystal of
diphenyl nitroxide (DPNO) doped in benzophenone (BzP),
1,3-bisdiphenylene-2-phenylallyl (BDPA) doped in polystyrene
(PS)
and
sulfonated-BDPA
(SA-BDPA)
doped
in
glycerol/water glassy matrices. In a sample of partially
deuterated PS doped with BDPA, we obtained an
enhancement of 323. Our findings demonstrate that NOVEL
pulse sequence is highly efficient, and can potentially surpass
routinely used continuous wave DNP mechanisms including
Page 89
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
the solid effect and cross effect both of which scale
unfavorably with magnetic field.
Poster 254
Constant-variable Flip Angle Gradient Echo for
Hyperpolarized Media MRI
He Deng; Jianping Zhong; Weiwei Ruan; Xianping Sun;
Chaohui Ye; Xin Zhou
Wuhan Inst. of Physics and Mathematics, CAS,
Wuhan, Hubei, China
Both the constant flip angle (CFA) scheme and the variable
flip angle (VFA) scheme could not maximally utilize the
hyperpolarization due to the nonrenewable hyperpolarized
magnetization and the limited breath holding time. A novel
constant-variable flip angle (CVFA) scheme, which combines
the advantages of CFA and VFA schemes, is presented to
maximize the usage of nonrenewable and limited
hyperpolarized magnetization. The presented scheme
suggests that hyperpolarized MR signals are acquired through
a train of n* CFA pulses, and then a train of N-n* VFA pulses.
The flip angle in CFA pulses, the number of CFA pulses, the
number of VFA pulses, and the initial variable flip angle in
VFA pulses are optimized to compensate the loss of
hyperpolarized magnetization.
Poster 255
Solution-State DNP at High Magnetic Field: Preliminary
Study from Relaxation in Supercritical Fluids
1
2
2
Adewale Akinfaderin ; Sungsool Wi ; Thierry Dubroca ;
2
2
3
Bianca Trociewitz ; Johan van Tol ; Lucio Frydman ;
2
Stephen Hill
1
2
Florida State University, Tallahassee, FL; National High
Magnetic Field Laboratory, Tallahassee, FL;
3
Weizmann Institute, Rehovot, Israel
One of the factors that cause inherent low enhancement in
solution-state DNP at high field is the solvent-solute
dynamics. In this study, we utilized supercritical fluids and
other organic solvents to understand how the relaxation
properties of small molecules depend on the solvent’s
viscosity. Some preliminary results that involve the use of a
high-pressure supercritical fluids cell assembly for high field
NMR and EPR spectroscopy will be presented and discussed.
From these experiments, we deduced the preeminence of the
spin rotation interaction and electron-proton dipolar interaction
on the spin-lattice relaxation rates.
Poster 256
Strategies for Membrane Protein Studies via
DNP MAS ssNMR
1, 2
1
2
Adam Smith ; Gail Fanucci ; Thierry Dubroca ;
2
1, 2
Stephen Hill ; Joanna Long
1
2
University of Florida, Gainesville, FL; National High
Magnetic Field Laboratory, Tallahassee, FL
Results of DNP MAS ssNMR experiments at 600 MHz/395
GHz, which combine the use of novel DNP instrumentation
and sample preparation strategies that aim to obtain structural
information from membrane protein systems will be
presented. We show that the DNP buildup time constant could
potentially be used as a measure of insertion depth of a
protein into a membrane. Also, we previously showed that by
incorporating the paramagnetic dopant within the membrane,
in the form of spin labeled lipids, we obtained more than two
times the DNP enhancement of a membrane embedded
peptide when compared to traditional sample preparations
Page 90
using water soluble biradicals. We are currently expanding
upon this sample preparation strategy by developing lipophilic
biradicals based upon cholesterol scaffolds.
Poster 257
A Novel photo-CIDNP Dye Tailored to the NMR Sensitivity
Enhancement of Low-Concentration Samples in Liquids
Yusuke Okuno; Silvia Cavagnero
University of Wisconsin-Madison, Madison, WI
Photo-chemically induced dynamic nuclear polarization
(photo-CIDNP) is a powerful hyperpolarization tool in NMR
spectroscopy. Given that liquid-state photo-CIDNP nuclear
spin polarization depends on a transient bimolecular chemical
reaction between a photoexcited dye and the sample of
interest, the extent of polarization is highly sampleconcentration dependent. Here we introduce fluorescein as a
novel photo-CIDNP dye whose features are exquisitely
tailored to samples at very low concentrations. We compared
the photo-CIDNP intensities of biological samples in the
presence of fluorescein or flavin mononucleotide (FMN) as
photosensitizers, and found that fluorescein yields superior
sensitivity enhancements down to the low micromolar sampleconcentration range. We propose that the observed excellent
behavior of fluorescein arises from its extremely long tripletstate lifetime and its superior photostability.
Poster 258
Effects of Strain and Confinement on Optical Dynamic
Nuclear Polarization in GaAs
1
1
2
John Tokarski III ; Ryan Wood ; Dipta Saha ; Lauren
1
2
3
3
McCarthy ; Gary Sanders ; Philip Kuhns ; Arneil Reyes ;
3
4
2
Stephen McGill ; John Reno ; Christopher Stanton ;
1, 2
Clifford R Bowers
1
Chemistry Department, University of Florida, Gainesville, FL;
2
Physics Department, University of Florida, Gainesville, FL;
3
National High Magnetic Field Laboratory, Tallahassee, FL;
4
Sandia National Labs, Albuquerque, NM
Poster 259
Bulk Nuclear Hyperpolarization in Diamond at High
Magnetic Fields
Melanie Drake; Eric Scott; Jeffrey Reimer
UC Berkeley, Berkeley, CA
High-Field OPNMR experiments with diamonds containing
several ppm of negatively charged nitrogen vacancy (NV-)
13
centers have generated bulk C spin polarizations of up to
0.1% at room temperature. The sign and magnitude of the
nuclear polarization is extraordinarily sensitive to the
orientation of the crystal with respect to B0. We discuss a
possible mechanism for this pumping process, which expands
upon a previous model that was based on an exchange of
energy between the NV- dipolar and nuclear Zeeman
reservoirs. The complex, heterogeneous nature of the system
has thus far precluded exact matches between the model and
data, but the expanded model accounts for positive and
negative nuclear polarizations and extreme sensitivity to
orientation.
Poster 260
Developments in NMR Signal Enhancement by Reversible
Exchange (SABRE): Nanoscale Catalysts for HET-SABRE
and A Water-Soluble Ir Catalyst for Aqueous SABRE in a
Single Step
POSTERS
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
1
2
2
2
Fan Shi ; Milton Truong ; Greg Zimay ; Aaron Coffey ; Roman
3
4
1
Shchepin ; Eduard Chekmenev ; Boyd M. Goodson
1
2
Southern Illinois University, Carbondale, IL; Vanderbilt
3
University, Nashville, TN; Vanderbilt University (VUIIS),
4
Nashville, TN; Vanderbilt University Institute of Imaging
Science, Nashville, TN
We report ongoing efforts to develop (1) nanoscale catalysts
for SABRE under heterogeneous catalytic conditions, and (2)
homogeneous catalysts for SABRE in aqueous environments.
For (1), TiO2/PMAA nanoparticle and PVP polymer comb
SABRE catalysts respectively provided up to ~(-)40-fold and
~(-)7-fold 1H signal enhancements for pyridine. The potential
for separation / reuse of catalyst particles is demonstrated.
For (2), pre-activation of the standard "[IrCl(COD)IMes]"
catalyst gives rise to an activated structure with much greater
water solubility. Subsequent re-constitution in water allowed
up to ~(-)33-fold 1H signal enhancements for nicotinamide. A
catalyst variant with a diol-funcionalized COD ring enables
aqueous SABRE in a single step without need for any organic
co-solvent; its utility for SABRE enhancement in water is
demonstrated.
Poster 261
Water Diffusion at the Micro to Nanoscale to Probe
Multiscale Network and Crowding by ODNP and PFG NMR
Ilia Kaminker; Kuoying Huang; Song-I Han
University of California Santa Barbara, Santa Barbara, CA
Nanometer scale water diffusion measured with Overhauser
Dynamics Nuclear Polarization employing trityl (ox63) radical
is compared with micrometer scale water diffusion as obtained
with Pulsed Field Gradient NMR. We demonstrate, for the first
time, that the two techniques provide similar results in
homogeneous solutions of trehalose, PEG and Ficoll across
wide range of bulk viscosities. Surprisingly diffusion as
obtained by PFG and ODNP did not correlate with known
viscosity values across these solvents in violation of the
Stokes-Einstein relationship, which predicts no dependence
on the nature of the viscogen. This suggests that the
molecular surfaces of the viscogens are affecting not only the
local water diffusivity, but also that of the hydration layer that
extends to beyond the angstrom lengthscale.
Poster 262
Development of Overhauser Dynamic Nuclear
Polarization at 14.1 T
1
1
2
Thierry Dubroca ; Bianca Trociewitz ; Adewale Akinfaderin ;
1
1
1
Hans van Tol ; Sungsool Wi ; William W. Brey ; Lucio
1, 3
1, 4
1, 2
Frydman ; Joanna R. Long ; Steve Hill
1
National High Magnetic Field Laboratory, Tallahassee, FL;
2
3
Florida State University, Tallahassee, FL; Weizmann
4
Institute, Rehovot, Israel; University of Florida,
Gainesville, FL
Dynamic nuclear polarization (DNP) is a novel technique
which has been shown to increase the sensitivity of high field
NMR (up to 18.8 T) by one to two orders of magnitude in
solids, but, in the liquid phase, 5 to 9.4 T DNP has only been
demonstrated in limited cases, and it has never been
demonstrated above 9.4 T. The National High Magnetic Field
laboratory is developing a new liquid solution DNP instrument
operating at 14.1 T. A gyrotron, the microwave source, is used
to polarized radicals' electron spins which in turn polarize the
spins of nuclei of interest, thus potentially providing large
NMR signal enhancements. We present here various
strategies to achieve Overhauser DNP at such a high field.
Poster 263
Achieving Very High DNP Enhancements in Frozen
Solutions at 9.4 T / 18.8 T and 100 K
1
2
3
Dominik J. Kubicki ; Aaron J. Rossini ; Claire Sauvée ;
3
3
Karthikeyan Ganesan ; Gilles Casano ; Martin
4
1
4
Schwarzwälder ; Moreno Lelli ; Copéret Christophe ; Armin
5
5
3
3
Purea ; Frank Engelke ; Olivier Ouari ; Paul Tordo ;
1
1, 2
Anne Lesage ; Lyndon Emsley
1
ISA, CNRS/ENS-Lyon/Université de Lyon, Lyon, France;
2
3
EPFL, Lausanne, Switzerland; CNRS UMR 7273, Aix4
Marseille Université, Marseille, France; Department of
5
Chemistry, ETH, Zürich, Switzerland; Bruker Biospin GmbH,
Rheinstetten, Germany
DNP currently attracts considerable attention as it has
recently evolved into one of the most efficient methods to
increase the sensitivity of MAS solid-state NMR spectroscopy.
With the recent introduction of high molecular weight
dinitroxides like TEKPOL or AMUPOL, signal enhancements
of between 100 and 200 are now routinely obtained at 9.4 T
and 100 K. These enhancement factors are however still far
from the predicted maximum values. We will report the DNP
performances of a total of 37 new nitroxides belonging to the
BTurea, PyPol, bTbK and TEKPOL series in frozen organic
solutions, and discuss the amplification effect observed upon
addition of solid dielectric particles into the sample. Results at
both 9.4 and 18.8 T will be presented.
Poster 264
Hyperpolarized Nanodiamond with
Long Spin Relaxation Times
Ewa Rej; Torsten Gaebel; Thomas Boele; David Waddington;
David Reilly
University of Sydney, Sydney, Australia
The use of hyperpolarized agents in Magnetic Resonance,
13
C-labeled compounds, enables powerful new
such as
imaging and detection modalities that stem from a 10,000-fold
boost in signal. A challenge for the hyperpolarization
technique is the inherently short spin-relaxation times,
13
typically <60 seconds for C liquid-state compounds, which
limit imaging time. Here, we demonstrate that 1.1% natural
13
abundance C spins in synthetic nanodiamond (ND) can be
hyperpolarized at cryogenic and room temperature without the
use of toxic free-radicals, and, exhibit relaxation times
exceeding 1 hour. Combined with the already established
applications of NDs as inexpensive fluorescent markers and
non-cytotoxic substrates for gene and drug delivery, these
results extend the capabilities of nanodiamonds into the
domain of hyperpolarized MR.
Poster 265
High Field DNP NMR of Biosilica-entrapped Enzymes
1
2
1
Vladimir K. Michaelis ; Enrico Ravera ; Eric Keeler ; Ta1
2
2
Chung Ong ; Tommaso Martelli ; Claudio Luchinat ;
1
Robert Griffin
1
2
Francis Bitter Magnet Lab, MIT, Cambridge, MA; CERM,
University of Florence, Sesto Fiorentino (FI), Italy
Solid-state NMR is a powerful technique for determining
chemical structure and dynamics. With the recent advances in
DNP NMR approach in conjunction with magic-angle spinning
challenging biological solids are now attainable. To further our
ability in understanding the biological molecule supported by a
Page 91
POSTERS
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
silicate framework and continue our DNP development efforts
we demonstrate the ability to hyperpolarize a series of
biosilica-entrapped enzymes. Various sample preparation
methods and contrasting DNP instrumentation (i.e., 211 MHz /
140 GHz v 699 MHz / 460 GHz) will be illustrated. DNP NMR
has enabled us to further our ability with magnetic resonance
offering new avenues once unimaginable.
Poster 266
Development of Immobilized SABRE Catalyst for
Continuous Hyperpolarization
Sören Lehmkuhl; Eva Paciok; Martin Wiese; Peter Schleker;
Matthias Wessling; Bernhard Blümich
RWTH Aachen University, Aachen, Germany
The SABRE (signal amplification by reversible exchange)
approach is an efficient hyperpolarization method enhancing
NMR signals by repeatedly transferring polarization from parahydrogen to target molecules using homogeneous Iridiumcomplexes.[1] Unfortunately these complexes are expensive,
usually inseparable for a reuse and potentially
disadvantageous for biological applications. Therefore
immobilizing these known homogeneous catalysts seems to
be a straight forward approach for new catalytic systems.[2] In
this project Iridium catalysts immobilised by polymer-bound
phosphine ligands are compared in a low-field NMR
spectrometer (42.5 MHz SpinSolve by Magritek Ltd.) in high
pressure NMR-tubes (up to 10 bar).[3] Current research
focuses on a combination of this approach with a micro fluidic
system to reveal the full potential of the promising results
shown in this study.
Poster 267
Investigation of the Kinetics of a Para-Hydrogenation and
Determination of the NMR Signal Enhancement per
Catalytic Cycle
Meike Emondts; P. Philipp M. Schleker; Bernhard Blümich
RWTH Aachen University, Aachen, Germany
Para-Hydrogen Induced Polarization, i.e. the hydrogenation of
unsaturated substrates with Para-Hydrogen, has proven to be
a valuable reaction in order to enhance the Nuclear Magnetic
Resonance (NMR) signal of the corresponding molecules and
to overcome the fundamental problem of low sensitivity of
NMR. During the hydrogenation reaction a high amount of the
initial para-hydrogen polarization seems to be lost due to
lower NMR signal enhancements than expected. Here, we
investigate the kinetics of hydrogenations by correlating the
NMR signal enhancement with the amount of hydrogenated
molecules within a specific time interval. We focus on the
influence of the kinetics on the signal enhancement factor by
varying ligands of a Rhodium catalyst.
Poster 268
Suppressing Solvent Signals in Dynamic Nuclear
Polarization (DNP) solid-state NMR via the Electronic
Mixing-Mediated Annihilation (EMMA) method
1
2
2
Fabio Ziarelli ; Giulia Mollica ; Pierre Thureau ; Fabien
3
2
Aussenac ; Stéphane Viel
1
2
Aix-Marseille Univ. & CNRS-FR1739, Marseille, France; AixMarseille Univ. & CNRS, ICR UMR 7273, Marseille, France;
3
Bruker Biospin SAS, Wissembourg, France
A simple procedure based on the so-called Electronic MixingMediated Annihilation (EMMA) methodology is shown here to
effectively suppress solvent signals in dynamic nuclear
polarization (DNP) solid-state NMR. These signals are
Page 92
present when analyzing samples prepared by glass forming or
incipient wetness impregnation, two common methods used in
DNP solid-state NMR for adding polarizing agents (e.g.
biradicals) to diamagnetic compounds. Similarly to the
TM
method, which uses an electronic signal as an
ERETIC
internal standard for quantification, EMMA is based on an
electronically generated time-dependent signal that is injected
into the receiver coil of the NMR probe head during the
acquisition. The phase of this electronic signal is shifted by
180° with respect to the receiver reference.
Poster 269
Investigation of Xenon Based Biosensors in an Aqueous
Oriented Environment
Clancy Slack; Ashley Truxal; Christophoros Vassiliou; Muller
Gomes; Phuong Dao; Keunhong Jeong;
David Wemmer; Alex Pines
UC Berkeley, Berkeley, CA
The detection of xenon in a functionalized molecular cage has
great potential in medical, environmental and material science
applications. The ability to produce simple clean spectra that
contain significant information about the molecular
environment makes xenon an excellent candidate for
performing noninvasive studies of complex mixtures. The
sensitivity of xenon to its chemical environment creates an
opportunity for significant sensitivity enhancement using
anisotropic environments such as DNA liquid crystals and
magnetically oriented bacteriophage. We have investigated
the effects of aqueous orienting environments on
cryptophane-based biosensors for the detection of molecular
binding.
Poster 270
New Applications of Dynamic Nuclear Polarization SolidState NMR to Materials Research
1
1, 2
1, 3
Takeshi Kobayashi ; Wenyu Huang ; Duane D. Johnson ;
1, 2
1, 3
1
Igor I. Slowing ; Vitalij K. Pecharsky ; Frederic Perras ;
1, 2
Marek Pruski
1
U.S. Department of Energy, Ames Laboratory, Ames, IA;
2
Department of Chemistry, Iowa State University, Ames, IA;
3
Department of Materials Science and Engineering, Ames, IA
We present several applications of SSNMR enhanced by
dynamic nuclear polarization (DNP) to the studies of new
materials in our laboratory. The studies include (1) host-guest
interactions between metal ions and MOFs, (2) thermolysis of
ammonia borane, (3) mechanisms of increased/decreased
DNP enhancement in the functionalized mesoporous silica
materials, (4) new types of heterogeneous catalytic materials
and cellulose, and (5) improved methods to polarize
quadrupolar nuclei under the DNP conditions.
Poster 271
Evaluating Carboxylesterase Activity with a
Hyperpolarized Xenobiotic Molecular Probe
1
1
2
Magnus Karlsson ; Pernille Rose Jensen ; Sonia Colombo ;
2
2
2
Claudia Cabella ; Luigi Miragoli ; Federico Maisano ; Fabio
2
1
Tedoldi ; Mathilde H. Lerche
1
2
Albeda Research, Copenhagen, Denmark; Bracco Imaging,
Colleretto, Italy
The idea of synthesizing ad hoc metabolically active
xenobiotics
for
metabolic
imaging
with
superior
hyperpolarization features is presented. A novel xenobiotic
13
molecule, 1,1-Cyclopropane-1- C-2,2,3,3-d4-di(methan-d2-ol),
1,1-diacetate (CDDA), has been specifically designed to
POSTERS
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
probe carboxylesterase activity and optimized for
13
hyperpolarized MRS applications. It features very long C
longitudinal relaxation time (T1), high solubility and very fast
conversion into the corresponding monoacetate (CDMA) and
dimethanol (CDM) derivatives. The metabolic fate of CDDA
has been investigated in rat liver and prostate cancer cells
and in vivo in rat prostate. Strong signals were recorded for
both the substrate and the hydrolyzed metabolites, which
were readily generated by intracellular carboxylesterases.
Poster 272
129
Temperature-Ramped Xe Spin-Exchange
Optical Pumping
2
2
Panayiotis (Peter) Nikolaou ; Aaron Coffey ; Michael J.
3
4
1
Barlow ; Matthew Rosen ; Boyd Goodson ;
5
Eduard Chekmenev
1
Southern Illinois University Carbondale, Carbondale, IL;
2
3
Vanderbilt University, Nashville, Tennessee; University of
4
Nottingham, Nottingham, UK; MGH/A.A. Martinos Center,
5
Boston, Massachusetts; Vanderbilt University Institute of
Imaging Science, Nashville, Tennessee
We describe temperature-ramped spin exchange optical
pumping (TR-SEOP) in an automated high-throughput batch129
Xe hyperpolarizer utilizing three key temperature
mode
129
regimes: (i) ‘hot’—where the
Xe hyperpolarization rate is
129
Xe hyperpolarization
maximal; (ii) ‘warm’—where the
129
approaches unity; and (iii) ‘cool’—where hyperpolarized Xe
gas is transferred into a Tedlar bag with low Rb content (<5 ng
per ~1 L dose) suitable for human imaging applications. The
variable-temperature approach increased the SEOP rate by
more than two fold compared to the constant-temperature
-3
-1
polarization rate (e.g. 62.5±3.7x10 min versus 29.9±1.2x10
3
-1
min ) while achieving nearly the same maximum %PXe
value (88.0±0.8% versus 90.1%±0.8%, for a 500 Torr (67
kPa) Xe cell loading—corresponding to NMR/MRI
5
8
enhancements of ~3.1x10 and ~2.32x10 at the relevant
fields for clinical imaging.
Poster 274
A Custom 200 GHz Gyrotron and DNP MAS Spectrometer
for Time Domain DNP and Electron Decoupling
1
1
1
Alexander Barnes ; Brice Albert ; Faith Scott ; Jagadishwar
2
1
1
1
Sirigiri ; Daniel Hoff ; Claire Derochers ; Eric Choi ;
1
Nicholas Alaniva
1
2
Washington University in St. Louis, St. Louis, MO; Bridge12
Technologies Inc., Framingham, MA
Cyclotron resonance masers (a.k.a. gyrotrons) are vacuum
electron devices capable of generating >100 W of millimeter
radiation for MAS DNP experiments at ~100 Kelvin. Extending
MAS DNP experiments to the time domain could have
substantial advantages such as improved performance at
higher temperatures and employing mounted mono-radicals
as polarizing agents, but requires pulsed or frequency swept
microwaves. Frequency control of microwaves could also
lead to effective electron decoupling schemes to reduce
paramagnetic relaxation effects (PRE). Here, we present
designs of a custom DNP MAS spectrometer which includes
1) a fast-frequency tunable gyrotron 2) a counter flow heat
exchanger for efficient cryogenic operation 3) a 5 frequency
NMR DNP probe, and 4) a DNP cryostat that
compartmentalizes DNP functions.
Poster 275
Tertiary versus Binary Gas Mixtures for Generating
Clinical-Scale Quantities of Hyperpolarized 129Xe via
Stopped-Flow Spin-Exchange Optical Pumping
1
2
1
Kaili Ranta ; Panayiotis Nikoloau ; Shawn Stephenson ;
1
1
2
Drake Anthony ; Brogan Gust ; Aaron Coffey ; Matthew
3
4
2
Rosen ; Michael J. Barlow ; Eduard Chekmenev ;
1
Boyd M. Goodson
1
2
Southern Illinois University, Carbondale, IL; Vanderbilt
University Institute of Imaging Science, Nashville, TN;
3
4
MGH/A.A. Martinos Center, Boston, MA; University of
Nottingham, Nottingham, UK
129
Xe by stopped-flow
In the preparation of hyperpolarized
spin-exchange optical pumping (SEOP), high resonant laser
fluxes are often used to overcome alkali metal spin
destruction from high xenon densities.
The resulting
increases in energy deposition can give rise to poorlyunderstood energy-transport and thermal dissipation
phenomena that can be difficult to manage. Given the high
thermal conductivity of helium and other advantageous
properties, we are investigating the use of tertiary gas
mixtures comprised of xenon, nitrogen, and helium and
comparing the results with our traditional binary gas mixture
comprised of only xenon and nitrogen. Experiments are
performed with our second-generation clinical-scale "XeUS"
xenon "hyperpolarizer". So far, addition of He leads to
modest reductions of PXe, but significantly faster "spin-up"
times.
Poster 273
Interplay of Catalyst Structure and Temperature for NMR
Signal Amplification by Reversible Exchange
1
2
3
3
Fan Shi ; Elizabeth Porter ; Milton Truong ; Aaron Coffey ;
3
3
1
Roman Shchepin ; Eduard Chekmenev ; Boyd M. Goodson
1
2
Southern Illinois University, Carbondale, IL; University of
North Carolina, Chapel Hill, NC;
3
Vanderbilt University, Nashville, TN
SABRE has many potential advantages for hyperpolarization
but is limited by the achievable polarization and the scope of
substrates. We investigate how catalyst choice can affect
resulting SABRE enhancements, including the interplay of
catalyst structure and temperature for optimal SABRE, as well
as catalyst activation. Results from the "standard" Ir SABRE
catalyst (1)—[IrCl(COD)(IMes)]—are compared with those
obtained with variants where –Cl is replaced with 4-aminopyridine, (diphenylphosphino)ethylamine, triphenyl phosphine,
or tribenzyl phosphine; a sixth variant was serendipitously
created by an alternate synthetic route for (1) that appears to
result in a polymorph according to x-ray crystallography.
Activation rate was inversely correlated with SABRE
enhancement, with peak 1H polarization enhancement (

ranging between ~(-)44 to ~(-)1900 at 9.4 T.
Page 93
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
SMALL MOLECULES
276 - 333
Poster 276
Reintroduction of Selective Scalar Interactions to a
Specific Proton in a Pure-Shift NMR Spectrum
Lokesh N; Sachin Rama Chaudhari;
Suryaprakash Nagarajarao
Indian Institute of Science, Bangalore, India
A new 1D NMR experiment cited as QG-SERF (Quick GSERF), which re-introduces selective proton–proton scalar
interactions to a specific proton in a pure shift NMR spectrum
during real time data acquisition, is reported. The method
provides information on multiple proton–proton couplings from
a single experiment, while significantly shortening the
experimental time by 1–2 orders of magnitude due to reduced
dimension and enhanced sensitivity.
Poster 277
In situ Ultrafast 2D NMR Spectroelectrochemistry for
Real-Time Monitoring of Redox Reactions
1, 2
1
1, 3
Patrick Giraudeau ; Renaud Boisseau ; Ugo Bussy ;
1
Mohammed Boujtita
1
2
Université de Nantes, Nantes, France; Institut Universitaire
3
de France, Paris, France; Michigan State University,
East Lansing, MI
The in situ combination of electrochemistry and NMR (ECNMR) is essential to elucidate in real time the mechanisms of
liquid-state redox reactions. We developed a 3-electrode
device fitting inside a 5 mm tube and coupled to a
potentiostat, making it possible to monitor redox reactions in
real time by liquid-state NMR. However, the implementation of
the electrochemical device inside the NMR probe induces line
broadening resulting in peak overlap. To deal with this issue,
we developed a method consisting in coupling EC-NMR with
ultrafast 2D spectroscopy, capable of recording 2D spectra in
a single-scan. This approach was successfully applied to the
real-time monitoring of fast redox reactions on small
molecules, leading to the identification of unstable
intermediates and reaction products.
Poster 278
13
15
HCNMBC: A Method for Measurement of C- N Coupling
Constants at Natural Isotopic Abundance
1
1
2
Steve F. Cheatham ; Michael Kline ; Eriks Kupce
1
2
DuPont, Newark, DE; Bruker Biospin, Coventry, UK
Analysis of a variety of heterocyclic systems using the
HCNMBC pulse sequence reveals consistent and diagnostic
patterns of correlations among the azoles.
We have
examined the dependence of cross peak intensity on the
13
15
setting of the JCN delay by direct measurement of the C- N
coupling constant at natural isotopic abundance. There are
13
15
two major ways of determining the C- N coupling – (1)
direct measurement in F1 and (2) analyzing signal intensities
as a function of the JCN delay.. Results from the examination
of a series of azoles using both methods and the applicability
13
15
of C- N coupling constants to structure elucidation will be
presented.
Page 94
Poster 279
Proton Deuteron Exchange for Aromatic Protons Under
Mild Conditions
Xiaohua Qiu
Dow Chemical Company, Midland, MI
Extensive hydrogen deuterium exchange was observed
between aromatic compounds with substituted electron
donating groups and D2O solvent under relatively mild
conditions typically employed for NMR spectroscopy. The
13
exchange was confirmed using mass spectroscopy, C NMR
1
spectroscopy, and H NMR spectroscopy. The influence of
the identity as well as the quantity of the electron donating
groups were investigated. To comprehend the temperature
1
effect on the exchange rate, H NMR was used to follow the
exchange kinetics at 5, 25 and 60 ˚C. An Arrhenius plot was
generated and an activation energy of 81 kJ/mol was
obtained.
Poster 280
Residual Dipolar Couplings and Residual Chemical Shift
Anisotropies for the Structural Discrimination of Small
Molecules
Nilamoni Nath; Edward J. d'Auvergne; Manuel Schmidt;
Christian Griesinger
Max-Plank Institute for Biophysical Chemistry,
Goettingen, Germany
For the conformational and configurational analysis of small
molecules, available one-bond Residual Dipolar Couplings
(RDC) may not be always sufficient when the molecule has
few C-H bonds. Complementary long range RDCs provide the
needed information to allow this under parameterized problem
to be solved. We present a method for extracting long range
RDCs and their analysis with a new alignment tensor
optimization tool and sign less J-couplings. In addition,
Residual Chemical Shift Anisotropy (RCSA) provides an
orientational sampling in the molecule and, importantly,
provides information about the quaternary and non-protonated
carbons. Application of RCSAs that are measured between
two alignment states in addition to long range RDCs analysis
will be presented for the discrimination of the configuration of
molecules.
Poster 281
Hydrolysis of –N=CH– bond in the 2-Salicylidine-4aminophenyl benzimidazole(SAPbzlH) using
Divalent Palladium
Chandrakala M
VV Pura College, Bangalore, India
The
Schiff
base,
2–salicylidene–4–aminophenyl
benzimidazole (I, SAPbzlH) in ethanolic medium reacts with
divalent palladium in acid medium (HCl/ HBr) and the
coordinated SAPbzlH undergoes hydrolysis at –N=CH– bond
to yield salicylaldehyde and square planar complexes of the
composition [Pd(C13H11N3)2X2].2HX (X = Cl, Br), II. The
complexes have been characterized by elemental analysis,
atomic absorption spectra (AAS), conductivity measurements,
infrared (IR), electronic and extensive NMR spectral studies.
Possible mechanism for the hydrolysis of coordinated
SAPbzlH has been proposed.
POSTERS
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
Poster 282
Reaction Monitoring by Desktop NMR Spectroscopy
1
1
Kawarpal Singh ; Ernesto Danieli ;
2
1
Yi-Qiao Song ; Bernhard Bluemich
1
RWTH Aachen University, Aachen, Germany;
2
Schlumberger-Doll Research, Cambridge, MA
Chemical reaction kinetics can be followed in real time by
NMR spectroscopy by passing the reaction mixture through
the magnet and acquiring spectra in stopped flow or
continuous flow mode. Due to shorter feed lines, desktop
NMR spectrometers provide better time resolution than highfield NMR spectrometers. Moreover, hazardous reactions can
be monitored by placing the instrument under the fume hood.
We report kinetic studies of a variety of chemical reactions
with time-resolved
single-shot 1H NMR spectroscopy
including first studies of the kinetic isotope effect, which aims
at understanding the chemically selective signature of
deuterium depletion in difference crude oils as this effect
reports on the evolution of the earth over a time range of up to
150 million years.
Poster 283
The BROCODE of NMR: BROadband COoperative
DEcoupling
1
2
2
Tony Reinsperger ; Franz Schilling ; Steffen Glaser ;
1
Burkhard Luy
1
KIT, Eggenstein-Leopoldshafen, Germany;
2
TUM, Garching, Germany
In heteronuclear correlation NMR, broadband decoupling
sequences are needed which provide high signal intensity
paired with low sideband artifacts. Up to recently it was bestpractice to pursue these goals in three steps:
1. Find a robust inversion pulse
2. Expand this pulse by phase cycling
3. Dynamically alter the timing of the sequence for
artifact cancellation
Maybe the best standard implementation addressing artifacts
originating from the three-step approach is adiabatic bilevel
decoupling.
Recently, methods based on Optimal Control algorithms have
been introduced that tackle all of the three above-mentioned
tasks simultaneously. In this work, we combine the Optimal
Tracking algorithm with multi-scan cooperativity in order to
derive a complete set of decoupling sequences that
compensate each other’s imperfections de novo.
Poster 284
Enhancing Sensitivity by 50-300% in Solution-State nJCH
Measurements and Applications to Unnatural Products
1
1
2
Craig P Butts ; Ikenna Ndukwe ; Godiraone Tatolo ;
1
1
Jessica Bame ; Stephanie Bull
1
2
University of Bristol, Bristol, UK; University of Botswana,
Gaborone, Botswana
Measuring nJCH - it should be easy, but it rarely is…..There
n
are a plethora of methods available for measuring JCH values
and it should be straight-forward to obtain these parameters in
principle. Unfortunately in practice it can be hard - especially
n
for the uninitiated. Yet when they are obtained, JCH values
can substantially improve the quality of analysis in challenging
dynamic structural elucidations. We employ F1-spectral
folding/deconvolution and F2-homonuclear decoupling to
massively enhance sensitivity (up to 300%) of EXSIDE-based
methods and demonstrate the significance of these
techniques by applying them to conformational analysis of
complex homologated alkane diastereomers.
Poster 285
Understanding Self-Assembly Process at Molecular
Level: Structure and Function of Guanosine Derivatives
1
2
Manjunatha Reddy G N ; Gretchen Marie Peters ; Lucia
3
2
3
Gramigna ; Jeffrey Davis ; Stefano Masiero ;
1
1
Andrew Marsh ; Steven Paul Brown
1
2
University of Warwick, Coventry, UK; University of Maryland,
3
College Park, MD; University of Bologna, Bologna, Italy
Nucleobases exhibit a rich supramolecular chemistry
predominantly imposed by non-covalent interactions. For
instance, lipophilic synthetic guanosine derivatives of
DNA/RNA bases self-assemble in organic solutions, on
surfaces and in the solid state. To explore this structural and
functional diversity, supramolecular chemists in Italy and the
US have joined Warwick to focus on a systematic
investigation of factors affecting self-assembly in guanosine
derivatives.
Poster 286
Sensitivity Enhancement of Slice-Selective NMR
Experiment by Adjacent Polarization Sharing
Lokesh N; Suryaprakash N
Indian Institute of Science, Bangalore, India
Slice selective NMR experiments provide multiple pieces of
information from a single experiment but at the cost of
sensitivity loss. Sensitivity of the experiment is critical issue
particularly in case of less concentrated solutions, such as,
natural products, metabolites and proteins. Therefore it is
significantly important to improve the sensitivity of slice
selective NMR experiments. In the present study we have
achieved an average of 2-fold sensitivity enhancement per
unit time. Adjacent polarization sharing technique was used to
transfer polarization from unused protons in each molecule to
selectively excited protons. This facilitates rapid data
acquisition without any customary inter-scan relaxation delay
and hence improved the sensitivity of the experiment per unit
time.
Poster 287
Real Time J-scaling in Nuclear Magnetic Resonance
Simon Glanzer; Klaus Zangger
University of Graz / Institute of Chemistry, Graz, Austria
Two of the main parameters in NMR spectra, which provide
structural information are chemical shift and scalar coupling
values. The resolution in the spectra can be enhanced by
scaling of the scalar coupling constants. Down-scaling of
scalar coupling values enhances the resolution of chemical
shift information and in the most extreme case leads to pureshift spectra. On the hand more accurate J values of well
resolved signals can be obtained by up-scaling of scalar
coupling. Here we presented pulse-sequences for real-time up
and down J-scaling. These novel pulse sequence elements
can be combined with 2D spectra to enhance or reduce
coupling constants in the direct dimension.
Page 95
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
Poster 288
Direct Measure of 1H Chemical Shift Tensors under Ultrafast MAS NMR for Polymorphic Distinction
1
1
2
Joshua Damron ; Kamal Mroue ; Manoj Pandey ; Kortney
1
2
1
Kersten ; Reddy Jayasubba ; Adam Matzger ; Yusuke
3
1
Nishiyama ; Ayyalusamy Ramamoorthy
1
2
University of Michigan, Ann Arbor, MI; CLST NMR Facility,
3
RIKEN, Yokohama, Japan; JEOL Ltd., Tokyo, Japan
Recent developments in magic angle spinning (MAS) NMR
probe technology have boosted the limit of spinning
frequencies up to 100 kHz and higher. In light of these
advances, it is now possible to obtain sufficiently narrow 1H
NMR lines in the solid-state, thus providing a unique
opportunity to directly measure various NMR parameters
including the 1H chemical shift anisotropy (CSA). We
demonstrate the measurement of 1H CSAs measured under
ultrafast MAS for polymorphic distinction of small organic
molecules
using
a
symmetry-based
2D
1H/1H
anisotropic/isotropic chemical shift correlation experiment.
The strong sensitivity of the 1H CSA to changes in intra- and
inter-molecular interactions provided structural insight into
polymorphic variation including hydrogen bonding and
electron interactions.
Poster 289
Carbon-multiplicity Editing in Long-range Correlation
NMR Experiments: Application to Natural Products
Josep Saurí
Merck, Rahway, NJ
A novel NMR method to obtain both long-range heteronuclear
correlations and carbon multiplicity information in a single
experiment, ME-selHSQMBC, is proposed. Even C/CH2 and
odd CH/CH3 can be directly distinguished from the relative
positive/negative phase of cross-peaks. The method can be
extended by a TOCSY propagation step via 1H-1H coupling
pathways, and it is fully amenable for the simultaneous and
precise determination of long-range heteronuclear coupling
constants.
ME-selHSQMBC spectra can become an important tool for
chemical assignment purposes and structure elucidation of
small molecules and natural products. Regarding the latter
application, some illustrative examples will be presented.
Poster 290
Structure Elucidation of a Proton-Deficient Natural
Product using LR-HSQMBC Supported by DFT
Calculations
Josep Saurí
Merck, Rahway, NJ
A severely proton-deficient marine alkaloid (C28H21N7O2)
was intractable to structural characterization using only
conventional 1D and 2D NMR techniques including HMBC
data which generally provides primarily two- and three-bond
correlations. A sensitive, complementary approach to obtain
very long-range (≥ 4JCH) heteronuclear correlations is
afforded by the recently reported LR-HSQMBC experiment.
LR-HSQMBC data were employed to gain access to
numerous 4JCH and several 5JCH heteronuclear coupling
pathways that were pivotal in linking together segments of the
alkaloid structure, which could not be accomplished solely
relying on HMBC data. The observed 4JCH and 5JCH
heteronuclear couplings were
Page 96
reasonable and consistent with DFT calculation of the
coupling constants and chemical shifts performed on the
proposed structure of the alkaloid.
Poster 291
Cryptospirolepine: Revisiting and Revising the Structure
Using Modern NMR Techniques, DFT Calculations, and
CASE Program Capabilities
Josep Saurí
Merck, Rahway, NJ
Cryptospirolepine is a complex indoloquinoline alkaloid
isolated in 1991. When the structure was reported in 1993, the
employed NMR methods were state-of-the-art, including 3mm
micro NMR probe technology. No 1H-15N HMBC methods
were developed yet. Some issues, such as the absence of
correlations to a carbonyl in HMBC data, among others, were
a concern regarding the structure elucidation. We have now
interrogated a 700 μg voucher sample of cryptospirolepine
using 1.7 mm MicroCryoProbe™ technology, 2 Hz optimized
1H-13C and 1H-15N LR-HSQMBC, newly developed pure
shift 1,1- and 1,n-ADEQUATE methods, DFT calculations,
and modern CASE methods. Using this powerful ensemble of
NMR experimental methods, state-of-the-art DFT calculations
and CASE methods, we now wish to report the revision of the
structure of cryptospirolepine.
Poster 292
Enantiomeric Interactions of Aminoacids Adsorbed in
Zeolites: An Investigation, using Solid-State NMR,
Thermogravimetry (TGA) and Differential Scanning
Calorimetry (DSC)
Deniz Cizmeciyan
Mount St. Mary's College, Los Angeles, CA
A new avenue to enantiomeric enrichment in zeolites is
important as a useful method in pharmaceutical industry. The
enantiomeric interactions between D and L amino acid
derivatives adsorbed in Zeolite NaY are investigated. As an
achiral structure, a zeolite does not favor one enantiomer over
the other. However, removing enantiomers at a 1:1 ratio will
result in an enantiomeric enrichment of a solution with a
preexisting enantiomeric imbalance. This enrichment could be
achieved when the D- and L-enantiomers are adsorbed as a
heterodimer. When adsorbed onto the zeolite, N-Acetyl
Methionine, N-acetyl-Alanine and N-Acetyl- Leucine exhibit
the same behavior indicating that they are adsorbed as
homodimers. NMR line widths show a 10 fold increase in
NaY indicating restricted molecular motion.
Poster 293
DNP Enhanced Solid-State NMR Spectroscopy:
Application to the study of Microparticles and
Polymorphs
1
3
1
Arthur Pinon ; Pierrick Berruyer ; Aaron Rossini ; Judith
2
3
4
Schlagnitweit ; Cory Widdifield ; Anne Lesage ; Lyndon
1
Emsley
1
2
EPFL, Lausanne, Switzerland; Johannes Kepler University
3
Linz, Linz, Austria; ENS Lyon, Villeurbanne, France;
4
University of Lyon, High Field NMR Center,
Villeurbanne, France
We present new developments in DNP enhanced MAS solidstate NMR for organic solids. Pharmaceutical compounds
often exist in different polymorphs, with different structures
and properties. Consequently, there is much interest in
characterizing the different polymorphs that might be present
POSTERS
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
in pharmaceutical formulations. However, the sample
preparation methods (grinding, impregnation) for DNP
experiments may themselves induce polymorphic changes.
Here we investigate these effects for several polymorphs of
theophylline, and show how we avoid phase changes.
We also turn our attention to characterizing the larger scale
phase structure in polymorphs and formulations. We show
how the spin diffusion properties that relay polarization from
the surface of organic particles to the core can be used to
measure domain sizes in polymer mixtures.
Poster 294
Site-Resolved Multiple-Quantum Filtered Distance
Measurements by Magic-Angle Spinning NMR: Theory
and Applications to Spins with Weak Quadrupolar
Couplings
Uzi Eliav; Amir Goldbourt
School of Chemistry, Tel Aviv University, Tel Aviv, Israel
In the current study we propose methods based on double
7
(DQ)- or triple (TQ)-quantum coherences of Li that are
obtained by the dipolar interactions via the formation of the
13
7
13
correlations Ix ( C)T2,0 ( Li) (resulting in DQ) and Iy ( C)T3, 0
7
( Li) (resulting in TQ). These methods were tested on the
+ model system [Li(GlyH)(H2O)] Cl . By fitting the experimental
results to either simulations or analytical expressions the
13
7
distance C- Li was obtained as well as an enhanced
7
resolution of the Li spectrum.
Poster 295
O NMR Studies of Lithium Based
Electrolytes
1
1
1
1
Mary Yang Hu ; Xuchu Deng ; Xiaoliang Wei ; Wei Wang ;
2
1
2
Zhong Chen ; Jun Liu ; Jian Zhi Hu
1
Pacific Northwest National Laboratory, Richland, WA;
2
Xiamen University, Xiamen, China
17
Natural abundance O NMR measurements were conducted
on electrolyte solutions consisting of Li[CF3SO2NSO2CF3]
(LiTFSI) dissolved in the solvents of ethylene carbonate (EC),
propylene carbonate (PC), ethyl methyl carbonate (EMC), and
their mixtures at various concentrations. It was observed that
17
O chemical shifts of solvent molecules change with the
17
concentration of LiTFSI.
Computational modeling of O
chemical shifts was carried out on proposed solvation
+
structures. It is found that a Li ion is coordinated with four
double bond oxygen atoms from EC, PC, EMC and TFSIanion. In the case of excessive amount of solvents of EC, PC
+
and EMC the Li coordinated solvent molecules are
undergoing quick exchange with bulk solvent molecules,
17
resulting in average O chemical shifts.
Natural Abundance
17
Poster 296
An Open Access NMR Database for Organic Natural
Products "CH-NMR-NP"
1
1
2
Kikuko Hayamizu ; Atsuko Yabe ; Katsuo Asakura ;
2
Tomomitsu Kurimoto
1
2
NMRDBTech, Tsuchiura, Ibaraki, Japan; JEOL Resonance
Inc., Tokyo, Japan
An NMR database for natural organic compounds ”CH-NMRNP” was opened as a freely accessible system from JEOL
RESONANCE website (www.j-resonance.com). Total number
of the compounds are about 30,500 compiled mainly from the
published papers from 2000 to 2014. Items for a compound
are Name, Molecular formula, Chemical structure with
13
1
assigment, the values of C and H shifts,
information,solvent, reference and others.
1
H-coupling
Poster 297
NMR Investigations of Densely Packed Vesicles
1
2
1
Felix Grewe ; Bruno Medronho ; Claudia Schmidt
1
2
University of Paderborn, Paderborn, Germany; University of
Algarve, Faro, Portugal
The aggregation of surfactants in aqueous solution often
leads to bilayers. Besides extended planar bilayers, vesicular
structures may form, in particular, when shear is applied.
Since diffusion parallel to the bilayers is much faster than
2
across, H NMR line shapes are affected by vesicle formation,
provided the quadrupole coupling matches with the diffusion
time scale. In dilute solutions, where the quadrupole couplings
of D2O are too small, NMR diffusometry can yield information
about vesicle formation. We will report on highly dilute
aqueous dispersions of 3 % sodium dodecyl sulfate (SDS)
plus fatty alcohol. Vesicular structures observed by
transmission electron microscopy at low SDS content are in
good agreement with our results of pulsed field gradient
diffusometry.
Poster 298
Diffusion NMR Measurements: An Efficient Tool for the
Analysis of Dynamic Systems Involving Paramagnetic
Lanthanide Complexes
1
1
Sandrine Denis-Quanquin ; François Riobé ; Marc-André
2
1
3
Delsuc ; Olivier Maury ; Nicolas Giraud
1
2
Laboratoire de Chimie, UMR5182, Lyon, France; IGBMC,
3
UMR7104, Illkirch, France; ICMMO, UMR8182,
Orsay, France
Lanthanide complexes are promising auxiliaries for protein
structure determination, since they combine luminescence
and anomalous scattering properties. In particular, trisdipicolinate complexes exhibit a strong affinity for cationic
amino acids. In previous studies combining NMR and
molecular modeling,
we characterized the interaction
between
[Ln(DPA)3]3and
small
molecules
like
EthylGuanidium that mimic the lateral chain of these amino
acids.
Diffusion experiments are a powerful tool to study
supramolecular complexes and can give access to numerous
information. Herein we report the measurement of diffusion
coefficients on a model lanthanide adduct [Na]3[Lu(DPA)3] to
evaluate the potential of this technique. Then, diffusion
experiments on [EtGua]3[Ln(DPA)3] demonstrate the ability of
monitoring small variations in dynamic systems using either
diamagnetic or paramagnetic metal ions.
Poster 299
13
Structural Characterization of U- C Labeled Small
Molecule Natural Products
1
1
2
2
Mikhail Reibarkh ; Gary Martin ; Tim Bugni ; Thomas Wyche ;
1
R. Thomas Williamson
1
2
Merck Research Labs, Rahway, NJ; University of Wisconsin
Madison School of Pharmacy, Madison, WI
Structure characterization of natural products was one of the
first applications of NMR spectroscopy. Over the years, the
process has evolved into a routine protocol that utilizes a set
of essentially standard NMR techniques. Although powerful,
this approach can be time-consuming and it sometimes leads
Page 97
POSTERS
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
to structural ambiguity, which had a negative impact on the
field of natural product research.
Here, we present a new approach to the rapid elucidation of
13
these molecular entities utilizing C labeling. This strategy
has recently become feasible due to the ready and
13
economical availability of U- C labeled substrates such as
glucose. We present an NMR protocol for the facile structure
13
elucidation of U- C labeled natural products and discuss the
selection of optimal NMR experiments.
Poster 300
Long Lived Coherences Excitation and Enhancement
1
1, 2
1
Riccardo Balzan ; Aude Sadet ; Laetitia Fernandes ; Fatiha
1
1
Kateb ; Paul Romeo Vasos
1
2
UMR 8601 - Université Paris Descartes, Paris, France; UMR
7203 - École Normale Supérieure, Paris, France
Long-lived coherences, LLC's, in pairs of coupled spins exhibit
longer relaxation times compared to T2 and are immune to
inhomogeneous broadening. This translates to sharp
resonances in the indirect dimension of multi-dimensional
experiments. Excitation of LLC's and LLS in pairs of quasiequivalent nuclei requires complex pulse sequences or the
use of sensitive spin locking.
We investigate LLC behaviour in presence of shifting rf
irradiation and show that, provided a third nucleus is
irradiated, broad band LLC excitation and enhancement can
be achieved for the two J-coupled spins. Similar observations
for long-lived states, LLS, and applications of LLC's and LLS
to dissolution-DNP enhanced NMR will also be discussed.
Poster 301
Exploring Long Lived States in Trans-Ethylene-D2
Zijian Zhou; Thomas Theis; Kevin Claytor; Warren Warren
Duke University, Durham, NC
Long lived states (LLS) with hyperpolarization can explore
slow chemical or metabolic processes. Here we explore the
use of pairs of deuterium atoms to provide access to LLS[1],
in this case, in nearby protons. As a first example, we show
that trans-ethylene-D2 has a proton LLS lifetime of 2 min
(8.5T, dissolved in hexane) despite T1 times of only 6s. The
advantage over previous work with such systems is that the
deuterium couplings make it possible to do storage and
readout with pulse sequences at any field strength.
Poster 302
Selecting Compounds to Serve as Standard Reference
Materials (SRMs) for Quantitative Nuclear Magnetic
Resonance (qNMR) Spectroscopy
Jason Widegren; Thomas Bruno
NIST, Boulder, CO
One of the great advantages of NMR spectroscopy is that,
with the proper choice of experimental parameters,
spectroscopic peak areas are proportional to the number of
nuclei that contribute to each peak. Therefore, the relative
concentrations of components in a mixture can be determined
directly from the spectrum. However, in order to perform a
qNMR experiment, in which the absolute amount of substance
is determined, a calibration is required. Currently, NIST does
not produce any SRMs that are certified for qNMR
spectroscopy, but we are in the early stages of developing
such SRMs. Selection criteria for the new SRMs will be
discussed. Initial data for purity, hygroscopicity, and stability of
six candidate compounds will be presented.
Page 98
Poster 303
CRAFT 2D Aids the NMR Structural Identification of a
Novel Diabetes Marker
1
1
2
Andrea M Sefler ; Anthony A Ribeiro ; Luke A D Miller ; Ann
2
2
M Evans ; Klaus-Peter Adam
1
2
Duke University, Durham, NC; Metabolon, Inc, Durham, NC
X12063 is a type II diabetes biomarker discovered in human
plasma by Metabolon. 50 ug has been purified for NMR
structural elucidation using the standard suite of 2D homoand heteronuclear sequences, e. g. TOCSY, HSQC, HMBC
and NOESY.
Overlapped methyl and methylene signals
complicate the identification of 2D cross peaks. 2D CRAFT
(Complete Reduction to Amplitude Frequency Table) was
used to further analyze the data. CRAFT 2D uses Bayesian
analysis to reconstruct FID models in f1.
A table of
frequencies, amplitudes and decay constants is obtained and
f1 is processed without apodization. Truncation effects in f1
are circumvented yielding higher quality 2D spectra. The
CRAFT reconstruction facilitates assignments in congested
regions and aids the structural identification of the biomarker.
Poster 304
NMR Structure Elucidation of Small Organic Molecules
and Natural Products: Choosing ADEQUATE vs HMBC
1
2
2
Alexei Buevich ; Thomas Williamson ; Gary Martin
1
2
Merck and Co., Kenilworth, NJ; Merck and CO., Rahway, NJ
Long-range heteronuclear shift correlation methods have
served as the cornerstone of modern structure elucidation
protocols for several decades. Despite the versatility and
extensive applications of the HMBC experiment, it can fail to
elucidate structures of molecules that are highly protondeficient.
In such cases, recourse to the ADEQUATE
experiments should be considered. The current study was
undertaken to facilitate a better understanding of situations
where it might be beneficial to apply 1,1- or 1,n-ADEQUATE
vs HMBC experiments to proton-rich and/or proton-deficient
molecules. Strychnine (1) and cervinomycin A2 (2) were
employed as model compounds for each of these structural
classes, respectively.
DFT methods were employed to
n
calculate the relevant heteronuclear proton-carbon JCH and
n
homonuclear carbon-carbon JCC coupling constants for this
study.
Poster 305
Stereochemical Characterization of Subtle Difference of
FIAU and FIRU, and Their Profound Different Biochemical
Toxicities
Qiuwei Xu
Merck Research Laboratories, West Point, PA
Fialuridine (FIAU) was developed and tested for the treatment
of Hepatitis B Virus (HBV) infection in the 1990s; but in early
clinical trials, it caused 5/15 patients death due to liver failure.
In this poster, we will present our NMR and in vitro cellular
toxicity work related to FIAU and its diastereoisomer FIRU.
Our NMR coupling constants of furanose, and hetero-nuclear
1H-19F NOEs helped characterize a compound labeled as
FIAU that turned out to be FIRU. Although FIAU and FIRU
have the same molecular weight, they showed very different
in vitro toxicity profiles.
Our work demonstrates the importance of stereochemistry
analyses for drug safety, and the dexterity of NMR for
POSTERS
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
stereochemcial characterization of compounds especially with
the same m/z.
Poster 306
Re-evaluating nOe Difference Spectra in View of
Improvements in NMR Spectrometer Stability
1
1
2
William F Reynolds ; Darcy C. Burns ; Ronald C. Crouch
1
2
University of Toronto, Toronto, Canada; NMR Consulting,
Loveland, CO
Acquiring nOe difference spectra by subtracting off- from onresonance irradiated spectra was, in the past, plagued by
subtraction artifacts. Consequently, this method has almost
entirely replaced by use of the DPF-SE sequence which gives
similar data but without artifacts. However, the latter sequence
does suffer from some sensitivity loss. Consequently, in view
of significant recent improvements in spectrometer stability.
we decided to re=evaluate the older method. We find that it
gives signal/noise about double that of the newer method,
often with acceptably low artifacts. Furthermore, artifacts can
entirely be avoided by directly comparing integrals form onand off-resonance spectra, taking advantage of the very flat
baselines produced by modern spectrometers.
Poster 307
Magic Angle Spinning NMR Studies on Guest-cage
Interactions in Clathrate Hydrates
1
1
Suvrajit Sengupta ; Jerry Jin Guo ;
1
1, 2
Kenneth Janda ; Rachel Martin
1
Department of Chemistry, University Of California, Irvine, CA;
2
Department of Molecular Biology and Biochemistry,
University of California, Irvine, CA
Clathrate hydrates are solid inclusion compounds, formed
when guest molecules such as methane, ethane, propane,
etc., occupy and stabilize host water cages under appropriate
temperature and pressure conditions. Though clathrate
hydrates have been studied extensively by X-ray, Raman
spectroscopy, NMR and other techniques, numerous
questions regarding the guest-cage dynamics still remain
unanswered. Tetrahydrofuran (THF) and cyclopentane (CP)
form CS-II clathrate hydrates. They only occupy the large
12 4
12 2
5 6 cages and leave the small 5 6 cages empty. They are
both five membered rings but THF has an oxygen atom which
is capable of forming hydrogen bonds. Here we employ MAS
ssNMR to compare the guest-cage interactions between THF
and CP hydrates, which will reveal the formation of hydrogen
bond in the future.
Poster 308
129
Functionalized Cryptophane as Xe MRI Probe for
Cysteine Tracking
Shengjun Yang; Weiping Jiang; Qing Luo; Qingbin Zeng;
Qianni Guo; Xin Zhou
Wuhan Inst. of Physics and Mathematics, CAS, Wuhan,
Hubei, China
Here, we present an acryloyl functionalized Cryptophane as
129
Xe MRI probe for the cysteine tracking in DMSO-aqueous
129
media (45:55 DMSO-HEPES buffer v/v, at pH 7.4). This Xe
probe was found to response fast with cysteine through
Michael addition reaction within a few minutes, and then
129
Xe chemical shift change. Moreover, it also
resulted in
shows highly selectivity toward cysteine over other amino
acids. Thus, this probe can be served as a new and very
promising sensor for rapid cysteine tracking in aqueous
solution.
Poster 309
14
High Resolution N-NMR Revisited
Benjamin Liu; Istvan Pelczer
Princeton University, Princeton, NJ
14
As N, which is a 99.7% natural abundance isotope of
nitrogen, has a quadrupolar moment, its NMR spectrum
usually has unbearably broad lines. However, when the
nitrogen atom has (at least nearly) symmetrical substitution,
this quadrupolar moment collapses, often resulting in sharp
lines.
14
Having in-house access to high quality probes suitable for N
1
detection at various fields (300, 500, and 800 MHz H
1
13
14
frequency), also including a custom-made H/ C/ N HRMAS, we have been exploring a large collection of nitrogen
containing compounds and have built an extensive database.
14
Next to direct detection of N, there exists a great possibility
to use inverse detection correlation methods regardless of
usually very small coupling constants involved. Both
approaches have been applied to various mixtures.
Poster 310
13
Predicting Functional Properties of Tablets with C13
Labeled Magnesium Stearate and C Solid-State NMR
Spectroscopy
1
1, 2
1
Sean Delaney ; Matthew Nethercott ; Nickolas Winquist ;
1
1
Manish Sethi ; Eric Munson
1
University of Kentucky, Lexington, KY;
2
Revolution NMR, Fort Collins, CO
Magnesium Stearate (MgSt) is a natural product that is added
as a lubricant to formulations in 0.25-1% to ensure the proper
ejection of tablets from a press. Pharmaceutical grade MgSt is
composed of the salts of stearic, palmitic, and other fatty acids
derived from natural sources. We have studied MgSt in tablets
13
by using 1- C stearic and palmitic acid to synthesize different
13
crystalline states of C-labeled MgSt. Even at 1% in the
formulation we could easily identify the structure of MgSt in
the tablet, and follow changes in the forms of MgSt upon
increasing blending time. Our ultimate goal is to correlate
NMR properties such as relaxation times and spectral
features of MgSt to functional properties of MgSt in tablets.
Poster 311
Line Narrowing in NMR Using Pathway Selective Pulses
1
2
1
Lauren F. O'Donnell ; Clark D. Ridge ; Jamie D. Walls
1
2
University of Miami, Coral Gables, Florida; United States
Food and Drug Administration, College Park, MD
The Pathway Selective Pulse (PSP) is a new pulse sequence
design methodology where any coherence and/or evolution
pathway selection scheme can be converted into a coherent
pulse which selectively excites a spin only if certain pathways
are available to it. A PSP based on reverse INEPT (RIPSP)
13
was presented where imperfections to C inversion pulses
1
13
are transformed via a combination of H and C pulses into
1
pure rotation of H spin magnetization in InS systems.
1
Application of RIPSP followed directly by H detection resulted
13
in 10-20% line narrowing in various C-labeled compounds
1
containing non chemically-equivalent H spins. Here we
present our current understanding of line narrowing under
RIPSP and propose a strategy to improve resolution in 1D
NMR experiments.
Page 99
POSTERS
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
Poster 312
Evaluation of Traces Intermediates in TPA Process
Technology using 1D & 2D NMR Spectroscopy
Dev Ranjan Pradhan
SABIC, Riyadh, Saudi Arabia
Terephthalic acid (TPA) is one of the most important
chemicals. TPA is the raw material of polyester
(PET).Accurately trace level identification and quantification
will help to qualify TPA process technology and to improve
their purification prior to use. A new, non-invasive and
operating at room temperature method have been developed
using NMR spectroscopic techniques. The method has been
applied successfully to crude TPA process system:
Terephthalic acid (TPA), 4-carboxybenzaldehyde (4-CBA) and
p-toluic acid as impurities. 1D (1H & 13C), DEPT NMR
techniques are used to identify the impurities in the presence
of the main TPA component. The results were confirmed by
2D NMR (COSY, HSQC & HMBC )spectroscopy. The each
identified NMR siganls were used to compute the amounts
upto trace levels
Poster 313
NMR Characterization of Benzoxazine Oligomers and
Polymers
Robert Webb
3M Corporate Research, St. Paul, MN
Benzoxazine resins are a novel class of thermosetting
polymers that have several commercially interesting
properties. The polymerization chemistry of benzoxazine
monomers, however, is not widely recognized or understood.
Cationic ring opening polymerization leading to traditional
polybenzoxazine structures is thought to dominate. NMR data
were collected as a function of degree of polymerization for
several pedagogical benzoxazine monomers. Modern NMR
methods have been utilized to characterize benzoxazine
oligomers and polymers that form.
Poster 314
Analysis of Agave Lignocellulosic Biomass through 2D
HSQC NMR Spectroscopy
Murali Dama
Postdoc, UC Berkeley, Berkeley, CA
Agave plant biomass is a potential biofuel feed stock. Here we
are analyzing the Agave lignocellulose composition through
2D HSQC NMR. The de-starched AIR material of Agave
biomass was ball milled and dissolved in a solvent containing
DMSO-d6 and small amount of ionic liquid ([Emim]OAc)-d14.
The relative monosaccharide composition (glucose, xylose,
arabinose, mannose and glucoronic acid) was quantified as
well as the H(p-hydrophenyl), S(syringyl) and G(guaiacyl)
lignin units. In addition the degree of acetylation of Xylan and
other wall polymers was quantified. Interestingly compared to
the other plant feed stocks the Agave base and tip contain low
amount of aromatic lignin (S, G, H) suggesting that such a
material should be easily saccharified for biofuel production.
Poster 315
The Intelligent NMR Spectrometer - Automatic Decision
Making for Structure Verification by NMR
1
1
1
2
Till Kuehn ; Jochen Klages ; Björn Heitmann ; Mark Garvey
1
2
Bruker Biospin AG, Fällanden, Switzerland; Bruker BioSpin
GmbH, Rheinstetten, Germany
In small molecule structure verification, one is confronted with
the problem, that a simple 1D proton spectrum may not yield
Page 100
the required information. In many cases further - and often
more time consuming - experiments are used or simply
solvent suppression etc. is required. Therefore very often
either only the 1D 1H experiments are run - which are in many
cases insufficient - or by default a whole suite of experiments
is run - whether useful or not. Here we presenet an innovative
solution that enables automatic on-the-fly decision making on
the NMR spectrometer to suggest the ideal combination of
experiments, taking into account the time available and
confidence required and we present a statistical evaluaton of
the automatically generated results.
Poster 316
Hadamard NMR with Multiple Receivers
1
1
2
Peter Gierth ; Anna Codina ; Frank Schumann ; Helena
2
1
Kovacs ; Eriks Kupce
1
2
Bruker Biospin, Coventry, UK; Bruker BioSpin AG,
Fallanden, Switzerland
We have adapted two PANSY (Parallel NMR SpectroscopY)
experiments – PANSY COSY and PANSY-TOCSY for
Hadamard encoding. The PANSY-TOCSY-Q experiment has
been modified to allow for simultaneous acquisition of three
different types of NMR spectra - C-13 of non-protonated
carbon sites, 2D TOCSY and multiplicity edited 2D HETCOR.
In addition the J-filtered 2D PANSY-gCOSY experiment
1
records a 2D HH gCOSY spectrum in parallel with a J-filtered
HC long-range HETCOR spectrum as well as offers a
simplified data processing. In favourable cases the total
recording time for the two PANSY experiments can be
reduced to just 40 seconds. The proposed Hadamard
encoded PANSY experiments provide sufficient information to
allow the CMC software package (Bruker) to solve structure of
small organic molecules.
Poster 317
Determination of an Intra-Ligand Distance for MembraneAssociated PKC C1b Domain-Bound Phorbol-12, 13Diacetate by REDOR NMR
1
2
2
Hao Yang ; Daryl Staveness ; Alison Axtman ; Alexander
1
1
2, 3
2
Barnes ; Jacob Schaefer ; Paul Wender ; Lynette Cegelski
1
2
Chem. Dept., Washington Univ., St. Louis, MO; Chem.
3
Dept., Stanford Univ., Stanford, CA; Chemical & Sys. Bio.
Dept., Stanford Univ., Stanford, CA
The interaction of Protein Kinase C (PKC) with native
physiological ligands drives fundamental cellular signal
transduction events. Aberrant PKC signaling is associated
with cancer, cardiovascular disease, neurological disorders,
stroke, and pain. Several drugs and emerging drug
candidates modulate PKC-mediated cellular activity and some
exhibit remarkable potential to ameliorate the adverse
consequences associated with disease. Yet structure-based
approaches are needed to better understand PKC-ligand
interactions in the membrane microenvironment to drive the
development of new therapeutic leads. We have interrogated
13
2
a three-component system comprised of a [ C, H3]-labeled
phorbol diacetate as a model ligand, complexed with the PKC
C1b domain in lipid vesicles and measured an intra-ligand
distance using REDOR NMR to report on the bio-active bound
conformation of the ligand.
Poster 318
CLIP-ASAP-HSQC for Fast and Accurate Extraction of
One-Bond Couplings from Isotropic and
Partially Aligned Molecules
POSTERS
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
Johanna Becker
KIT, Eggenstein-Leopoldshafen, Germany
We introduce the CLIP-ASAP-HSQC experiment that allows
fast acquisition of spectra with clean inphase multiplets in 25
seconds. The performance in terms of precise extraction of
one-bond couplings is demonstrated on three test samples
including partially aligned molecules.
Poster 319
RDC-Based Structure Elucidation of
Flexible Small Molecules
Burkhard Luy
KIT, Karlsruhe, Germany
A pulse sequence on the way to semi-automated coupling
determination derived from basic principles of optimum control
of quantum systems will be shown as a prerequisite for
effective coupling measurement. As the main aspect it will be
shown that time-averaged molecular dynamics with dipolar
couplings as full orientational restraints can be used to solve
problems in small molecules without the need of introducing
an explicit molecular alignment tensor in the computations.
Poster 320
Structural Features of Azumamide Analogues by NMR
Spectroscopy
1
2
1
Casper Hoeck ; Alex R. Maolanon ; Jesper S. Villadsen ;
1
1
2
Niels J. Christensen ; Peter Fristrup ; Christian A. Olsen ;
1
Charlotte H. Gotfredsen
1
Technical University of Denmark, Kgs. Lyngby, Denmark;
2
University of Copenhagen, Copenhagen, Denmark
The 3D structural features of azumamides, a group of nonribosomal cyclotetrapeptides, were investigated due to their
HDAC inhibition. Solution structures of a natural azumamide
were compared to a series of unnatural analogues, varied by
2
removal or inversion of a β -methyl group; a group conserved
among natural azumamides.
The 3D structures were all evaluated by NOEs using the
isolated spin pair approximation and J-coupling constants
using Karplus and Haasnoot-de Leeuw-Altona equations to
retrieve distances and dihedral angles respectively. Effects of
conformational averaging were shown to have a large impact
on the obtained spectroscopic data, and thus the resulting 3D
structures. Diversity in the structural features was found in
2
between the structures; mostly in the vicinity of the β -methyl
group.
Poster 321
BB-SAT-DQF-COSY---New Broad Band Saturation DQFCOSY to Saturate Huge Water and Sugars and to Observe
Minor Components in Foods
1
2
3
Kazuo Furihata ; Chiseko Sakuma ; Mitsuru Tashiro
1
2
University of Tokyo, Bunkyo-ku, Tokyo, Japan; Tokyo
University of Pharmacy and Life Sciences, Hachiouji, Tokyo,
3
Japan; Meisei University, Hino, Tokyo, Japan
In many foodstuffs, the signals of water and sugars make the
minor components undetectable or detected with very low
sensitivity due to the limitation of dynamic range. BB-WET
method has already been reported as a robust method for
broad band saturation. Although the decent 1D-1H NMR
spectra were obtained, its application to DQF-COSY was
unexpectedly difficult. Most of the phase cycles were not
useful, resulting in the artifact peaks. we have developed a
new technique, Broad Band Saturation(BB-SAT)-DQF-COSY.
The proposed method was applied to saturate the resonances
of water and sugars simultaneously in a sample of pineapple
juice. In a DQF-COSY spectrum, in which both water and
sugar resonances were saturated, cross peaks of minor
components were successfully observed.
Poster 322
Poster 323
An NMR Investigation of Atropisomerism in Ortho
Substituted 1,1-dibromo-2,2 diphenylcyclopropane
1
1
Narasimhamurthy Shanaiah ; Amanda Nelson ; Neeraj
2
1
1
Patwardhan ; Carla Slebodnick ; Paul Carlier ;
1
Webster Santos
1
Department of Chemistry, Virginia Tech, Blacksburg, VA;
2
Department of Chemistry, Duke University, Durham, NC
In our efforts to synthesize a library of 1,1-diaryl allenes from
gem-dihalocyclopropanes as substrates, we explored the
dynamic behavior of ortho substituted 1,1-dibromo-2,2
diphenylcyclopropane (1) using NMR. The compound 1 in
solution is a challenging NMR puzzle exhibiting atropisomeric
properties, a rare example of restricted rotation about an (aryl)
C(sp2)–C(sp3) bond featuring a cyclopropyl ring. Application
1
of Variable-temperature 1D and 2D- EXSY H NMR
measurements for compound 1 in CDCl3 over a range of
temperatures (30 to -30 ˚C) together with a detailed analyses
resulted in the two interconverting systems. The heights of
two different rotational barriers have been calculated and
these experimental findings are in close agreement with DFT
calculations.
Poster 324
Differentiation of Racemic Mixtures and Meso
Compounds using Chiral Alignment Media
Malin Reller
Karlsruhe Institute Of Technology, Karlsruhe, Germany
The unambiguous assignment of racemic mixtures or meso
compounds is up to date a challenging field of research. We
will present novel experiments based on different ways to
correlate the two parts of a molecule across the symmetry
center using isotropic mixing and residual dipolar couplings in
chiral environments.
Poster 325
Extensions and Limits of the ASAP-HSQC
1
2
David Schulze Sünninghausen ; Johanna Becker ;
1, 2
Burkhard Luy
1
Institut für Organische Chemie, KIT, 76131-Karlsruhe,
2
Germany; IBG 4 - Magnetische Resonanz, KIT, 76344Eggenstein-Leopoldshafen, Germany
Previously we introduced the ASAP-HSQC as a fast
method for the detection of heteronuclear single quantum
coherence spectra of small molecules at natural abundance.
Here we are exploring the limits of the experiment by
combining the ASAP approach with other time saving
techniques. This allows the acquisition of HSQC spectra in a
couple of seconds. Further developments of the experiment
will be presented, which include for example a multiplicity
edited version of the sequence.
Poster 326
Simple and Precise Measurement of Heteronuclear
Coupling Constants by Novel Broadband Homonuclear
Decoupled NMR Methods
Page 101
POSTERS
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
1
2
2
István Timári ; Ralph W. Adams ; Mathias Nilsson ; Tünde Z.
1
1
2
1
Illyés ; László Szilágyi ; Gareth A. Morris ; Katalin E. Kövér
1
University of Debrecen, Institute of Chemistry, Debrecen,
2
Hungary; University of Manchester, School of Chemistry,
Manchester, UK
A variety of novel methods have been developed in recent
years that reduce the complexity of 1H NMR spectra by
collapsing the multiplet structure of each resonance into a
singlet. These experiments deliver pure chemical shift
information without the complication of homonuclear coupling
interactions and with significantly increased resolution in the
direct proton dimension.
Implementing
broadband
homonuclear
decoupling
methodology in the CLIP/CLAP-HSQC[1] and HSQMBC[2]
experiments the undesired proton-proton splittings are
removed from the heteronuclear multiplets, thus the
heteronuclear couplings of interest can be determined simply
by measuring the frequency differences between the peak
maxima of pure doublets.[1] I. Timári et al., J. Magn. Reson.
2014, 239, 130-138. [2]
I. Timári et al., Chem. Eur. J. 2015,
21, 3472-3479.
Poster 327
Resolution of Flavanone Epimer Mixtures by NMR and
Matrix-Assisted DOSY
2
1
1
Rosa Estrada-Reyes ; Héctor Luna ; Aida Solís ; Herminia
1
3
1
Pérez ; Yann Prigent ; Julia Cassani
1
Universidad Autónoma Metropolitana, México, D.F;
2
Laboratorio de Fitofarmacología, INPRFM, México, D.F,
3
México; Univ Toulouse, Toulouse, France
The study of complex mixtures by NMR is a growing research
area, and includes methodologies for the analysis of plant
extracts as well as other types of mixtures. The detailed
structural analysis of flavonoid glycoside mixtures has shown
special complexity. However, flavanone glycosides present
epimer signals, which are in the region around 5.5 and 2.6
ppm corresponding to protons of the Carbons 2 and 3, which
are slightly separated from the others. We present results
using trifluoroacetic acid (TFA) in order to induced better
diffusion for Matrix-Assisted DOSY (MAD) experiment, in
addition, TFA induced a favorable dispersion of signal and
helped to stabilize epimer interchange.
Poster 328
Homonuclear Decoupling by Projection Reconstruction
1
2
1
Benjamin Görling ; Wolfgang Bermel ; Stefan Bräse ;
1
Burkhard Luy
1
2
KIT, Karlsruhe, Germany; Bruker BioSpin, Rheinstetten,
Germany
We present an experiment that is a modified version of the
HR-HMBC to reduce signal overlap in the direct dimension. It
also uses pulses derived from optimal control of quantum
systems for improved robustness. Separation is achieved by
exploiting the J-resolved like tilt of the HMBC. Due to scalable
evolution time, the tilt becomes scalable as well and can be
adjusted to the specific problem. Since all signals in a specific
experiment exhibit the same tilt, a projection approach is
introduced to collapse the multiplet patterns along this tilt to
singulets. Because of the scalable tilt, projection with different
angles can be obtained and a virtually homonuclear
decoupled spectrum can be generated by backprojection of all
projections.
Page 102
Poster 329
High Pressure NMR: Ethylene Glycol as a NMR
“Barometer” and Reversible Pressure Dependent
23
Quadrupolar Coupling of Na in Pf1 Bacteriophage
Joshua Steele; James B. Ames; Matthew Augustine
University of California Davis, Davis, CA
High pressure nuclear magnetic resonance (NMR) is a
promising technique to investigate molecular scale structural
changes in chemical and biological systems. Ethylene glycol
1
is found to be a suitable NMR “barometer” by measuring H
chemical shift differences as a function of pressure. This
chemical shift difference is also used to estimate the +5 K
temperature change due to compression heating during
sample pressurization to 2,000 bar. A reversible pressure
23
dependence of the Na residual quadrupolar coupling is also
reported in magnetically aligned Pf1 bacteriophage. The
mechanism for this coupling recycling is probed by comparing
measurements to simple electrolyte screening models.
Poster 330
A Clean in-Phase COSY Experiment
Martin Koos; Burkhard Luy
Karlsruhe Institute of Technology, Karlsruhe, Germany
The COSY-experiment is one of the oldest 2D NMR
experiments; yet, it is still invaluable for the assignment of
1
signals in H spin systems, showing only coherences between
directly coupled spins and providing cross peaks of high
explanatory power.
We present a novel experiment to overcome its major
drawback: the anti-phase line shape. The clean in-phase
COSY (CLIP-COSY) yields purely absorptive cross peaks for
the same coherences. It allows short acquisition times and is
less prone to mismatched processing parameters while
providing full resolution of phase-sensitive spectroscopy.
The line shape is strongly dependent on the properties of a zfilter element applied. To explore the limits of such elements,
we utilized the GRAPE algorithm, an implementation of
optimal control theory on quantum systems.
Poster 331
PF-06767669, an Adduct of CP-690550 and Acrolein,
Structure Elucidation by NMR
Fangming Kong
Pfizer, Groton, CT
Tofacitinib (CP-690,550) is a drug (trade name XELJANZ) of
the janus kinase (JAK) inhibitor class. In the development
phase of the ophthalmic drop formulation, a low level
degradant at 0.8% in 25C/12 months clinical stability sample
was observed. The degradant was found to be present in foil
pouch specific to one vendor.
Foil pouch’s adhesive
decomposition product acrolein was suggested to be the root
cause. Acrolein spike into the formulation confirmed that the
degradant is an adduct of acrolein and API. Detailed
analyses of the NMR data led to the structure determination of
PF-06767669 to be a hemiaminal compound with its nitrogen
atom (N-20) positively charged. Both MS and NMR spectra
are consistent with the structure.
Poster 332
Automated Structure Verification: What are the Right
Experiments and Processing?
1
1
Sergey Golotvin ; Rostislav Pol ;
2
3
Philip Keyes ; Patrick Wheeler
POSTERS
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
1
2
ACD Moscow, Moscow, Russian Federation; Lexicon
Pharmaceuticals, Princeton, New Jersey;
3
ACD Labs, Toronto, Ontario
Standard structure characterization regularly employs a
variety of 2D NMR techniques. However, past practice for
Automated Structure Verification (ASV) primarily employs
1
1
either 1D H NMR only, or a combination of 1D H NMR and
1
13
2D H- C HSQC. Recent work makes the inclusion of a wide
array of experimental data possible in ASV work. This poster
presents an analysis of the value of different correlation
techniques in order to better understand the value of various
experiments in ASV work.
Poster 333
Development and Evaluation of Experiments for
Oligosaccharide Structure Elucidation Using
Phosphitylated Derivatives
1
2
Clark D. Ridge ; Eugene Mazzola
1
2
FDA, College Park, MD; University of Maryland,
College Park, MD
Oligosaccharides can be difficult to characterize by NMR due
to the crowded proton spectrum. Spectral overlap and strong
coupling can make it difficult to separate out the ring-proton
multiplets, which are important for determining the protonproton coupling constants used to identify the sugar subunits
of oligosaccharides. Structural elucidation of such compounds
can be aided by applying the NMR experiments developed for
carbon-13 labeled derivatives to oligosaccharides derivatized
with a phosphorous labeling scheme originally used in the
quantitative analysis of edible oils. The main advantage of
using the phosphorous derivatization is the speed of the
reaction. The acetylation and sample clean-up can take up to
24 hours. The phosphitylation reaction can be done in a few
minutes in an NMR tube.
DRUG DISCOVERY
334 - 344
Poster 334
Fingerprinting Higher Order Structure of Protein
Therapeutics
Leszek Poppe
Amgen Inc., Thousand Oaks, CA
The need for robust Higher Order Structure (HOS) assays has
increased as regulatory agencies move to create abbreviated
pathways for the approval of “biosimilar” biological products.
Arguably, Nuclear Magnetic Resonance is the single most
preferred method for fingerprinting the higher order structure
of a protein in solution, typically by recording 1H-15N or 1H13C correlation spectra. Here, we propose that the PROFILE
approach (L. Poppe et al. Analytical Chemistry 2013, 85,
9623-9629), which is based on 1D 1H NMR, is superior to
typical two-dimensional NMR methods. We demonstrate this
for a glycoprotein and antibody protein therapeutics.
Poster 335
Drug Discovery Efforts Against TrkA
Hugh Eaton; Mark McCoy
Merck Research Labs, Kenilworth, NJ
We show how NMR methods are used to support both the
discovery of 1) antibodies that target the extracellular TrkAd5
domain and 2) small molecules that target the intracellular
kinase catalytic domain of the TrkA receptor.
Poster 336
Characterization of Compounds that Prevent Aggregation
of the Intrinsically Disordered Protein Tau by NMR
1
1
2
Hai-Young Kim ; Mark McCoy ; Shahriar Niroomand ; Michael
2
1
1
Rudd ; Daniel Wyss ; Corey Strickland
1
2
Merck, Kenilworth, NJ, USA; Merck, West Point, WP, USA
Aggregation of the microtubule-associated protein Tau into
filamentous inclusion bodies is a characteristic event in
Alzheimer's disease (AD). Inhibition of this protein misfolding
and aggregation is a potential mechanism to modify the
underlying disease mechanism. We used NMR to evaluate a
representative member of the two novel uHTS-identified
chemical series both chemically and mechanistically. The
residues that interact with MB and the two potent Merck
Research Laboratory (MRL) Tau aggregation inhibitors have
been determined, including Cys291, Cys321, and the VQIVYK
hexapeptide motif that promotes aggregation. In summary we
have provided mechanistic insights into MRL compounds
inhibiting Tau aggregation; specific modification of the native
cysteine residues retains Tau in a monomeric conformation
preventing the formation of filaments and their toxic
precursors.
Poster 337
NMR Methods for Characterization of Protein
Therapeutics at Natural Isotopic Abundance
Luke Arbogast; Robert Brinson; John P. Marino
IBBR-NIST, Rockville, MD
Methods for facile characterization of the higher order
structure of protein therapeutics are in great demand for
establishing consistency in drug manufacturing and
comparing biosimilars to innovator reference products. In
principal, NMR can provide a robust approach for such
characterization; however the perceived need for stable
isotope labeling has limited its use to date. We describe
experimental methods for the collection and analysis 1H-15Namide and 1H-13C-methyl correlations spectra on natural
abundance protein therapeutic samples, including monoclonal
antibodies, using standard and rapid acquisition techniques.
Results will be presented that demonstrate the precision and
resolution with which these methods can be used to
characterize the structure of formulated biotherapeutics and
establish statistical structural comparability between drug
samples.
Poster 338
MRI-visible Liposome Nanovehicles for Highly Efficient
Delivery of Theranostic Agents
Lili Ren; Shizhen Chen; Haidong Li; Zhiying Zhang; Xin Zhou
Wuhan Inst. of Physics and Mathematics, CAS, Wuhan,
Hubei, China
Real-time diagnosis and monitoring of disease development,
and therapeutic responses to treatment, are possible using
theranostic magnetic resonance imaging (MRI). Here we
developed a multifunctional liposome, containing Gd-DOTA
and paclitaxel. This nanoparticle overcame the insolubility of
paclitaxel, reduced the side effects of FDA-approved
formulation of PTX-Cre (Taxol®) and improved the drug
delivery efficiency to the tumor. c(RGDyk) modification greatly
enhanced the cytotoxicity of the drug to tumor cells A549. In
vivo, the tumors in mice were visualized using T1-weighted
imaging after administration of the liposome. Fluorescence
images in vitro and ex vivo also showed the targeting effect of
Page 103
POSTERS
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
this liposome in tumor cells. These findings lay the
foundations for the further application of this delivery vehicle
in cancer therapy settings.
Poster 339
Structure and Mechanism of Protein–Nanoparticle
Interactions: Insights from NMR Spectroscopy
Somnath Mondal; Thirupathi Ravula; Kousik Chandra;
Hanudatta Sastry Atreya
Indian Institute of Science, Bangalore, India
In recent years, graphene-oxide(GO) and its derivatives have
emerged as efficient nanomaterials for drug delivery.
However, to design GO based drug delivery systems it is
important to understand its interaction with proteins in biofluids. We have chosen the globular protein ubiquitin for
studying its interaction with GO. Using 2D-NMR spectroscopy,
we have probed the structure and dynamics of interaction of
ubiquitin with GO. It is observed that the conformation of
ubiquitin is un-altered during its interaction with GO, but there
is strong broadening of signals of the protein, which is not
significant in the case of an intrinsically disordered protein.
This implies the importance to consider both the conformation
and dynamics of the protein to understand its interaction with
GO.
Poster 340
Pharmaceutical Formulation Development of the New
Long-acting Recombinant Human Insulin Analog SK3R by
NMR and MS
Elzbieta Bednarek; Jerzy Sitkowski; Wojciech Bocian; Lech
Kozerski
National Medicines Institute, Warsaw, Poland
We have designed a new promising human insulin analog
SK3R which characterizes a long-acting, flat, almost no
“peakless” course of regulating glucose in time and showing
no fluctuations on concentration during long-term
administration. These properties of SK3R insulin seem to be
superior than commercial products and therefore SK3R
insulin was selected for research and development of
pharmaceutical formulation. The right choice of the
composition and physico-chemical properties of the
pharmaceutical form is very important. This may strongly
affect the agglomeration properties and finally the
pharmacokinetics. The determination of the oligomeric
composition of SK3R in the proposed pharmaceutical
formulations was achieved by PFGSE NMR experiments and
nanospray ESI MS. Studies were performed by changing:
ionic strength and concentration of formulation components.
Poster 341
Fragment-based and Structure-aided Discovery of HIV-1
Glycoprotein 41 Fusion Inhibitors
1
1, 2
Shidong Chu ; Miriam Gochin
1
2
Touro University, Vallejo, CA; UCSF, San Francisco, CA
HIV-1 gp41mediates viral membrane fusion and represents an
ideal target for HIV entry inhibitor discovery. Currently no
effective small molecule fusion inhibitors exist.
We employed a fragment-based approach to gp41 inhibitor
discovery, using a specifically designed assay and ligandbased NMR screening. We identified several hits that bind to
a conserved hydrophobic pocket on the NHR coiled coil of
gp41, or to an adjacent C-terminal sub-pocket. PRE assisted
docking was used to identify possible binding modes of
Page 104
ligands in each pocket. These may be used to assist
development of strategies to tether the fragments into a
larger, more active inhibitor.
The hits were also used to
characterize novel protein constructs developed to form stable
trimers with exposed binding surfaces for small molecules.
Poster 342
Novel Swapped Domain Structures of the
gp41 Ectodomain
1
1, 2
Shidong Chu ; Miriam Gochin
1
2
Touro University, Vallejo, CA; UCSF, San Francisco, CA
HIV-1 gp41 mediates viral membrane fusion and represents
an ideal target for discovering HIV entry inhibitors. Currently
no detailed structural data exist for gp41 : small molecule
complexes, a limiting factor for structure-based drug design.
To get more structural/mechanistic understanding the small
molecule gp41 inhibitors developed in our group,
we
designed and prepared a series of new gp41 ectodomain
reverse hairpins, with the CHR domain preceding a loop and
the NHR domain. Biophysical characterization including CD,
NMR and analytical ultra- centrifugation confirmed that the
proteins formed stable trimers in solution with exposed
binding surfaces for small molecules. The effect of DPC on
the structure of the hairpins was also investigated, in order to
mimic the membrane environment of gp41.
Poster 343
Discovery of New Leishmania donovani Nucleoside
Hydrolase Inhibitors by Molecular Fragment and Natural
products using STD NMR
Marina Alves; Charlotte Nirma; Lidia Lima; Luzineide Tinoco
UFRJ, Rio De Janeiro, Brazil
Nucleoside hydrolase (NH) enzyme is a target for the
development of drugs to treat leishmaniasis. To identify new
substances able to inhibit Leishmania donovani NH (LdNH),
we are using two approaches based on the use of STD NMR
technique: the molecular fragment based drug discovery and
the screening of Brazilian Atlantic Forest’s plants extracts. 129
molecular fragments library was created based on the rule of
three and the structural similarity with NH substrates. These
fragments were tested using STD and 12 showed LdNH
interaction, some of them with IC50 in the range of µM. 180
plants extracts were previously evaluated by enzymatic assay
and the 7 that inhibiting NH activity in 50 % or more were
evaluated by STD.
Poster 344
NMR Solution Structure of AMPK β1 CBM and
Identification of Its Binding Interactions with Activator
A769662
Hong Wang
Pfizer, Groton, CT
AMP-activated protein kinase (AMPK) is a central monitor and
regulator of cellular metabolism and energy status in
mammalian cells. Activators of AMPK have long been sought
as a therapeutic approach for diabetes and cancer. To help
understand how the A769662 type small molecule activators
interact with AMPK, we used NMR to investigate its
interaction with a Carbohydrate Binding Module (CBM) of
human AMPK. We were able to clearly detect interactions
between A769662 and an isolated CBM of the human AMPK
isoform through 15N-1H chemical shift perturbation. We
determined the solution structure of the human CBM and
identified important interacting regions on the CBM structure
POSTERS
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
based on chemical shift mapping and mutagenesis and
functional assays.
METABOLOMICS
345 - 366
Poster 345
Absolute Quantitative Metabolomics of Plant Extracts by
Fast 2D NMR
1, 2
1, 3
3,
Patrick Giraudeau ; Tangi Jézéquel ; Catherine Deborde
4
3, 5
3, 4
; Mickaël Maucourt ; Annick Moing
1
2
Université de Nantes, Nantes, France; Institut Universitaire
3
de France, Paris, France; Plateforme Métabolome Bordeaux4
MétaboHUB, Villenave d'Ornon, France; INRA UMR 1332
Biologie du Fruit et Pathologie, Villenave d’Ornon, France;
5
Université de Bordeaux, Villenave d'Ornon, France
Quantitative 2D NMR is a powerful tool for targeted
quantitative metabolomics, but conventional experiments
suffer from long experiment durations leading to a limited
precision. Recent stategies derived from ultrafast 2D NMR
offer a promising alternative, as they are capable of recording
2D spectra of biological material in a few minutes with an
excellent precision. Here, we show that such hybrid
strategies,
associated
with
interleaved
acquisition
approaches, can be used to monitor the evolution of major
metabolite concentrations in tomato extracts corresponding to
different fruit development stages.The changes observed in
metabolite levels during the fruit development and ripening
are fully consistent with the metabolism of tomato. The results
show that fast 2D methods form a promising tool for fast
targeted metabolomics.
Poster 346
Comprehensive Multiphase (CMP) NMR Monitoring of the
Molecular Flux within a Growing Seed
1
1
1
Blythe Fortier-Mcgill ; Leayen Lam ; Ronald Soong ; Ries de
4
1
2
2
Visser ; Myrna J. Simpson ; Werner E. Maas ; Michael Fey ;
4
2
2
Antonie Gorissen ; Howard Hutchins ; Jochem Struppe ;
2
3
3
Sridevi Krishnamurthy ; Rajeev Kumar ; Martine Monette ;
3
1
Henry J. Stronks ; Andre J Simpson
1
2
University of Toronto, Toronto, Canada; Bruker Biospin
3
Corp., Billerica, MA; Bruker BioSpin Canada, Milton, Canada;
4
IsoLife BV, Droevendaalsesteeg, The Netherlands
Comprehensive Multiphase (CMP) NMR probes introduced in
2012 are capable of monitoring the flux of both the
metobolome and structural components (both semi-solid and
solid), thus offering unprecedented opportunities to expand
our understanding of biochemical pathways. Here, we
demonstrate the potential of the CMP probes, by monitoring
13
changes within a growing C labelled seed. We found that the
triacylglyceride (TAG) signal, decreased by 65 %, 37 % and
34 % at 96 h relative to the 0 h (dry seed), for metabolites with
unrestrictive diffusion, those with restrictive diffusion and
semi-solid components, respectively. For the anomeric carbon
signals of the carbohydrates—including D-xylose, D-raffinose,
sucrose and glucose—there was an increase of 260 %, 380 %
and 390 %, respectively.
Poster 347
Multi-phase Comprehensive Analysis of a
Living Organism
1
1
Yalda Liaghati Mobarhan ; Blythe Fortier-McGill ; Ronald
1
2
2
2
Soong ; Werner Maas ; Michael Fey ; Jochem Struppe ;
2
2
3
Howard Hutchins ; Sridevi Krishnamurthy ; Rajeev Kumar ;
3
3
1
Martine Monette ; Henry Stronks ; Andre Simpson
1
2
University of Toronto, Toronto, ON; Bruker BioSpin Corp.,
3
Billerica, MA; Bruker BioSpin Canada, Milton, ON
Comprehensive Multiphase (CMP) NMR is used to study all
components (liquids, gels, and solids) in vivo for the first time.
Due to its wide use in aquatic toxicity testing fresh water
shrimp Hyalella Azteca is studied. The full range of
components, from rigid polysaccharides (chitin in the shell) to
soluble metabolites, are studied and fully differentiated using
spectral editing approaches. Soluble metabolites provide an
information-rich molecular fingerprint that can help explain
biochemical fluxes induced by environmental stressors.
Similarly gels (i.e. membranes, proteins) and solids (i.e. cell
walls, shells) hold the potential to comprehend changes to the
structural framework of a living system. When all phases are
considered synergistically CMP-NMR provides a unique and
comprehensive insight into in-vivo structure and processes.
Poster 348
NMR Based Metabolic Profiling to Identify Biomarkers in
the Serum of Patients with Takayasu’s Arteritis (TA)
1
1
2
1
Cl Khetrapal ; Anupam Guleria ; Durga Misra ; Atul Rawat ; R
2
3
1
N Misra ; Paul Bacon ; Dinesh Kumar
1
Centre of Biomedical Research, Lucknow, Uttar Pradesh,
2
India; Department of Immunology, SGPGIMS, Lucknow,
3
Uttar Pradesh, India; Department of Rheumatology,
Birmingham University, Birmingham, UK
Takayasu’s arteritis (TA) is a rare, systemic, chronic
inflammatory disease of unknown aetiology. Here, we have
compared serum metabolic profiles of 52 TA patients with
those of 32 normal healthy individuals using 1D 1H NMR, 2D
1H-13C HSQC NMR (at 800 MHz) and multivariate data
analyses.
The results reveal an altered lipid metabolism in TA patients
as inferred by significantly decreased levels of lipid
metabolites and acetate (an end product of lipid metabolism)
in the serum samples of TA patients. Additionally, the serum
level of N-acetyl-Aspartate was found to be significantly
elevated in TA patients. The study shows correlation with the
severity of the disease and provides novel insights into the
metabolic changes associated with it.
Poster 349
A New NMR-Based ATP Assay for Studies of
Mitochondrial Functions
Liping Yu
University of Iowa, Iowa City, IA
Interpreting mitochondrial function as affected by comparative
physiologic conditions is confounding because individual
functional parameters such as ATP production, oxygen
consumption, membrane potential, and generation of reactive
oxygen species (ROS) are interdependent. Here, we have
developed a new, highly sensitive, and specific NMR-based
assay to quantify ATP production of isolated mitochondria
under clamped levels of membrane potential. We have used
a 2-deoxyglucose (2DOG) energy clamp to set the membrane
potential at fixed levels and to quantify ATP production via
measuring the conversion of 2DOG to 2DOG-phosphate using
NMR spectroscopy. We have applied this assay to study
muscle, liver, and heart mitochondrial function of control
versus diabetic mice fed under different diets and
antioxidants.
Page 105
POSTERS
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
Poster 350
Dissolution Dynamic Nuclear Polarization Studies of Cell
Cultures
James Collins; Joanna Long; Daniel Downes; Bimala Lama
University of Florida, Gainesville, FL
Dissolution DNP greatly enhances the potential of NMR
studies of in-vitro cell culture studies, due to the large (>
15,000) increase in 13C signal. One of the major challenges is
the transitory nature of the hyperpolarized signal, which
rapidly returns to its equilibrium value. By focusing on specific,
rapid, metabolic pathways, significant information regarding
cell behaviour can be obtained. Initial experiments have been
conducted on E. coli grown in minimal media, and in the
stationary growth phase. In these experiments hyperpolarized
Sodium [1-13C] Pyruvate, and the resulting metabolic
products were monitored. Work is ongoing to use a range of
hyperpolarized metabolites to study both E. coli and human
breast cancer cells, and the effect various growth conditions
have on them.
Poster 351
NMR on the Micron Scale: Pipeline for Metabolomic
Profiling of C. elegans
Christoph Trautwein
University of Freiburg, IMTEK, Freiburg, Germany
Minimizing sample volume in NMR addresses two of its main
limitations: enhancing sensitivity and efficient use of precious
samples. However, what is established for standard NMR
does not necessarily translate to µ-NMR. Dealing with
metabolite concentrations in the mM to µM range in µL
volumes requires the adaptation of several standard
procedures. The following workflow pipeline reflects
experiences from own research and peer-reviewed literature
and aims to instruct users in the performance of metabolomic
µ-NMR experiments from the beginning of sample separation
until statistical data evaluation. We will present a collection of
tips-and-tricks for proceeding through all steps in the
presented pipeline.
Poster 352
1
Potential Role of H NMR Spectroscopy of Seminal
Plasma of Cow-Bull to Identify Sub-Fertility:
Preliminary Results
1
1
2
Virendra Kumar ; Pawan Kumar ; Khushpreet Singh ; N. R.
1
2
Jagannathan ; Ajeet Kumar
1
Department of NMR, All India Institute of Medical, New Delhi,
2
India; Department of Vet. Gynae. and Obst., GADVASU,
Ludhiana, India
Seminal plasma of bulls contains a mixture of secretions.
Characterization of metabolites in seminal plasma may help to
identify biochemical biomarkers related to fertility of bulls. In
present study we are using various NMR methods to
investigate the biochemical profile of seminal plasma which
could help differentiation between cow-bulls having good
fertility and poor fertility. Differences in the intensities of
metabolite like Citrate and some amino acids are noticed. The
results revealed altered metabolism resulting change in the
concentration of the metabolites evident in seminal plasma.
Further work is in progress to identify more number of
metabolites using 2D NMR techniques and rigorous statistical
analysis including multivariate tests like principal component
analysis.
Page 106
Poster 352
13
Cerebral Metabolism of Focally Administered 2,3- C2
Succinate in Human Traumatic Brain Injury: A
Microdialysis and High Resolution NMR Study
1
1
1
Ibrahim Jalloh ; Keri L.H. Carpenter ; Peter Grice ; Duncan J.
1
1
3
1
Howe ; Andrew Mason ; Clare N. Gallagher ; Adel Helmy ;
2
1
1
Michael P. Murphy ; David K. Menon ; T. Adrian Carpenter ;
1
1
John D. Pickard ; Peter J. Hutchinson
1
2
University of Cambridge, Cambridge, UK; MRC
3
Mitochondrial Biology Unit, Cambridge, UK; University of
Calgary, Calgary, Canada
Following traumatic brain injury (TBI), high brain extracellular
lactate/pyruvate (L/P) ratio suggests high glycolytic activity,
correlating with unfavourable outcome. We investigated
whether focal administration of succinate, a tricarboxylic acid
(TCA) cycle intermediate interacting directly with the
mitochondrial electron transport chain, could improve brain
energy metabolism. We used microdialysis to perfuse
13
disodium 2,3- C2 succinate (12 mmol/L) for 24h into 6 TBI
patients'
brains
and
simultaneously
collected
the
microdialysates for analysis (13C NMR and ISCUSflex clinical
13
13
analyzer). Products included 2,3- C2 malate and 2,3- C2
13
glutamine indicating TCA cycle metabolism, and 2,3- C2
lactate suggesting TCA cycle spinout of pyruvate and
conversion to lactate. Compared with baseline, succinate
perfusion improved brain chemistry: lower L/P ratio (due to
higher pyruvate), lower glutamate, and better glucose
utilisation.
Poster 354
1H-NMR Profiling Predicts Rituximab Therapy Outcome in
Rheumatoid Arthritis
1
1
1
Shannon Sweeney ; Alessia Lodi ; Bo Wang ; Arthur
2
2
2
1
Kavanaugh ; David Boyle ; Monica Guma ; Stefano Tiziani
1
2
University of Texas at Austin, Austin, TX; UC San Diego
School of Medicine, La Jolla, CA
Nuclear magnetic resonance (NMR) spectroscopy has been
investigated as a clinical tool for disease diagnosis and
characterization of drug response in several systems. We
assessed the ability of high-resolution 1H-NMR to detect
differences in metabolic profiles between rheumatoid arthritis
(RA) patients who did and did not respond to rituximab
therapy. Multivariate analysis of the 1H-NMR spectra
positively discriminated between rituximab responders and
non-responders, as classified by their ACR20 score. Prior to
treatment, we found several metabolites that contributed to
significant differences between groups. As expected, blood
metabolic profiles changed following treatment, suggesting a
metabolic shift in response to treatment. These data suggest
that 1H-NMR may be a useful tool to predict treatment
outcome in RA patients prior to administration.
Poster 355
NMR Profiling of Extracellular Metabolic Flux in Breast
Cancer Cells
Avigdor Leftin; Rui Simoes; Suresh Veeraperumal; Ellen
Ackerstaff; Jason Koutcher
Memorial Sloan Kettering, New York, NY
Metabolites serve as biomarkers for evaluating factors that
promote, or reduce cancer cell growth. Evaluating many
combinations of cells and drugs presents a combinatorial
problem that challenges conventional large-scale highresolution NMR approaches. We implemented a high-
POSTERS
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
resolution NMR protocol that enables high-throughput
measurements of in vitro extracellular flux and validated the
measurements with human and murine breast cancer cell
lines subject to microenvironmental stress, and metabolic
cancer therapy. The technique was tested both at natural
1
13
isotopic abundance with H-NMR, and with stable C isotope
tracers. Profiles of metabolite concentrations and fluxes were
obtained in response to drugs and hypoxia. These findings
motivate the use of faster and more sensitive approaches for
measuring metabolic flux in high-throughput formats to
accelerate cancer research.
Poster 356
Diffusion-Enhanced USPIO Relaxivity of
Biomolecular Metabolites
Avigdor Leftin; Jason Koutcher
Memorial Sloan Kettering, New York, NY
Ultrasmall superparamagnetic iron oxide nanoparticles
(USPIO) shorten transverse relaxation times via an outersphere relaxation mechanism. As this mechanism is
dependent on the diffusion coefficient of the molecular
species detected, we wished to explore whether detecting
metabolites instead of water could increase the apparent
relaxivity of these particles. We combined T2 CPMG and
bipolar
pulsed-field
gradient
diffusion
coefficient
measurements to evaluate relaxivities in metabolite
phantoms. Dextran-coated 5nm USPIO particles affected the
relaxivity of metabolites by a factor of 2-3 fold over water, in
proportion to their diffusion coefficient. The relaxivities were
further enhanced by changing the viscosity of the medium.
These results indicate that USPIO relaxivity is influenced by
molecular diffusion, and more sensitive detection can be
achieved using metabolite signals.
Poster 357
Development of a Combined 13C NMR and LC-MS Method
for Unknown Metabolite Identification
1
1
1
Chaevien Clendinen ; Gregory Stupp ; Bing Wang ; Timothy
2
1, 2
Garrett ; Arthur Edison
1
2
UF/NHMFL, Gainesville, FL; Southeast Center for Integrated
Metabolomics, Gainesville, FL
Compound identification in metabolomics is a challenging
problem. We have recently demonstrated that Isotopic Ratio
Outlier Analysis (IROA), an untargeted LC-MS metabolomics
method, can determine the molecular formula and fold-change
of metabolites in response to a perturbation. We demonstrate
an approach using high-sensitivity 13C NMR to identify an
unknown metabolite from a fraction isolated from an IROA LCMS experiment. We were able to obtain close matches of two
of the unknown fragments to NMR databases containing
anthranilic acid and glucose, and chemical shift calculations
were utilized to determine the correct isomer. This approach is
efficient and can be used to identify unknown compounds of
interest using the same material used for IROA.
Poster 358
Determining the Metabolic Changes by siRNA Treatment
for Ovarian Cancer Using Nuclear Magnetic Resonance
Jaehyuk Lee; Niki Millward; Rajesha Rupaimoole; Anil Sood;
Pratip Bhattacharya
The University of Texas MD Anderson Cancer Center,
Houston, TX
NMR based metabolic profiling provides an excellent
biomolecular method to access response of new treatment
siRNAs for ovarian cancer. We compared the expression of
metabolites for cultured ovarian cells (SKOV8) in vitro and
orthotopic animal models in vivo with different siRNA
treatments between controlled and treated groups in several
metabolites such as lactate, acetate, formate and creatine.
The results show high-resolution NMR can provide a
comprehensive and complete overview of the entire
metabolite compositions and distinguished efficacy of
treatment for in vitro and in vivo samples. This NMR based
metabolomics is a powerful tool to measure the metabolic
changes to access tumor progression as well as the efficacy
of new therapy and drug response in ovarian cancer.
Poster 359
Expanding the Limits of Human Blood Metabolite
Quantitation using NMR Spectroscopy
1
2
1, 3
G. A. Nagana Gowda ; Yashas Gowda ; Daniel Raftery
1
2
University of Washington, Seattle, WA; Purdue University,
3
West Lafayette, IN; Fred Hutchinson Cancer Research
Center, Seattle, WA
The reliable and quantitative determination of many
metabolites in blood is a current challenge in metabolomics.
Focused on alleviating this bottleneck, we have developed a
sample preparation approach that allows the identification of
67 blood metabolites by NMR, along with comprehensive
peak annotations for easy metabolite identification. Further
investigations of quantitation using organic solvents revealed
a surprisingly poor performance for protein precipitation using
acetonitrile and optimal performance for 2:1 methanol.
Further, the ability to quantitatively evaluate nearly 70 blood
metabolites, which represent numerous functional groups,
using a simple analytical method such as NMR will allow the
evaluation of samples for analysis across many samples and
different analytical platforms, including mass spectrometry.
Poster 360
Massive Glutamine Cyclization to Pyroglutamic Acid in
Human Serum Discovered Using NMR Spectroscopy
1
2
1, 3
G. A. Nagana Gowda ; Yashas Gowda ; Daniel Raftery
1
2
University of Washington, Seattle, WA; Purdue University,
3
West Lafayette, IN; Fred Hutchinson Cancer Research
Center, Seattle, WA
Utilizing a recently developed approach [Anal. Chem.
87(1):706-15, 2015] that offers access to an unprecedented
number of quantifiable blood metabolites, a surprising
glutamine cyclization to pyroglutamic acid is identified.
Interestingly, while glutamine cyclization occurs in both
ultrafiltered and protein precipitated serum, the cyclization
was not detected in intact serum. Strikingly, due to cyclization,
the apparent serum glutamine level drops by up to 75% and,
concomitantly, the pyroglutamic acid level increases
proportionately. Further, the magnitude of cyclization is vastly
different for different portions of the same pool of serum.
However, the sum of glutamine and pyroglutamic acid
concentrations in each portion remains the same. These
findings indicate the importance of accounting for this
unexpected phenomenon in the metabolomics of blood.
Poster 361
Analysis of the Effects of Multi-generational and TransGenerational Prenatal Stress on Urinary Metabolite
Profiles Using 1H NMR Metabonomics
Douglas Kiss; Mirela Ambeskovic;
Gerlinde Metz; Tony Montina
Page 107
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
University of Lethbridge, Lethbridge, Canada
Chronic exposure to stress during pregnancy produces a
unique uterine environment that reprograms the fetal HPA
axis and alters the epigenome. These changes manifest as
behavioral and psychiatric disorders throughout the lifespan of
the offsping. Our research is motivated by previous findings
demonstrating the trans-generational transmission of
epigenetic factors resulting from prenatal stress. We collected
urine samples from a model of prenatal trans-generational
and multi-generational stress and analyzed the urinary
metabolic profile of the F4 offspring. By following basic
metabonomic protocols we were able to identify distinct
metabolic profiles associated with both trans-generational and
mulit-generational prenatal stress. These profiles will now be
compared with epigenetic, behavioral, and other data in an
attempt to identify molecular mechanisms driving changes.
Poster 362
Preliminary Studies of the Enzymatic Pentose Phosphate
Pathway using Dissolution Dynamic Nuclear Polarization
1, 2
1, 2
3
Emeric Miclet ; Aude Sadet ; Aurélien Bornet ; Jonas
3
3
1, 2
Milani ; Sami Jannin ; Geoffrey Bodenhausen ; Daniel
1, 2
Abergel
1
2
Univ. Pierre et Marie Curie, Paris, France; Ecole Normale
3
Supérieure-PSL, Paris, France; Instit. des Sciences et
Ingéniérie Chimiques, EPFL, Lausanne, Switzerland
Dissolution Dynamic Nuclear Polarization (D-DNP) has
proven a very efficient hyperpolarization technique. Many
applications have emerged, among which the study of
metabolic processes in cell suspensions or living tissues. To
date, only a limited number of in vitro D-DNP NMR studies
aiming at the investigation of enzyme kinetics have been
performed. We have recently undertaken the kinetic study of
Glucose phosphorylation by Hexokinase using D-DNP
experiments. Using a simple kinetic model, we have been
able to describe the reaction in the absence or presence of a
an inhibitor. More recently, we have focused on the next stage
of the Pentose Phosphate Pathway. The associated
preliminary results will be presented, as well as technical and
methodological issues raised by these experiments.
Poster 363
Urine Metabolomics: A Potential Approach to Diagnose
and Monitor Multiple Sclerosis
1
1
Teklab Gebregiworgis ; Chandirasegaran Massilamany ;
1
1
2
Arunakumar Gangaplara ; David Stteffen ; Helle Nielsen ;
2
1
1
Zsolt Illes ; Jay Reddy ; Robert Powers
1
2
University of Nebraska-Lincoln, Lincoln, NE; University of
Southern Denmark, Odense, Denmark
NMR metabolomics was used to study urine metabolite
signatures associated with Multiple Sclerosis (MS). MS is a
very challenging disease to diagnose where delayed and
misdiagnosis is common. This delay is also detrimental to a
successful treatment outcome for MS, since treatments are
more effective during the early course of the disease when
symptoms are mild. The study was conducted using
Experimental Autoimmune Encephalomyelitis (EAE) mice.
Our approach identified a diverse set of metabolites that can
be used to differentiate between healthy and EAE mice. A
clinical study is currently in progress to identify urine
metabolite signatures from MS patients. The approach has a
promise for providing fast and safe method for diagnosing MS
and monitoring the effectiveness of treatments.
Page 108
Poster 364
Holistic Assessment of the Biological Effects of NanoDrug Carrier and Beneficial Effects of the
Nano-Encapsulated Drugs
1
2
1
1
1
Yipeng Song ; Ruifang Zhao ; Yili Hu ; Fuhua Hao ; Ning Li ;
2
3
1
Guangjun Nie ; Huiru Tang ; Yulan Wang
1
CAS Key Lab MR Bio Syst, Wuhan Inst Phys Math, Wuhan,
2
China; National Center for Nanoscience and Technology,
3
Beijing, PR China; School of Life Sciences, Fudan University,
Shanghai, PR China
Nanoparticle encapsulated doxorubicin (DOX) and paclitaxel
(TAX) has the potential to treat cancer. However, the safety of
nanoparticle
material,
methoxypoly(ethylene
glycol)poly(lactide-co-glycolide) (mPEG-PLGA) and the effects of
mPEG-PLGA packed DOX and TAX are not fully asserted.
We applied NMR-based metabonomics to characterize the
systemic metabolic changes associated with mPEG-PLGA
and nano-drugs exposure. The result shows that mPEGPLGA exposure act as a transient stimulus toward the host. In
addition, mPEG-PLGA packaging can reduce toxicity of the
drugs, which particularly manifested in heart and liver.
Furthermore, nano-drugs exposure induces shifting in energy
metabolism, stimulates anti-oxidation of system and disturbs
gut microbial activity of host. These findings provide a holistic
insight in the biological effect of polymer nanoparticles and
nanoparticle encapsulated drugs.
Poster 365
Reproducibility and Time Dependence of Metabolites in
1
Serum by H NMR
1
1
1
Matthew M. Miele ; Broc R. Wenrich ; Rajasri Alaparthi ; Brian
2
1
A. Irving ; David Rovnyak
1
2
Bucknell University, Lewisburg, PA; Geisinger Medical
Center, Danville, PA
Traditional strengths of profiling metabolites by NMR include
unambiguous identification of metabolites while avoiding
variation in results due to column performance and sample
preparation. These advantages are more commonly noted
anecdotally while there appears to be less investigation on
fundamental validation and reproducibility of NMR-based
metabolite measurements. This work reports quantitative
analyses of NMR metabolite profiling of extracted serum
samples with emphasis on three areas: (i) day-to-day and
replicate reproducibility, (ii) time dependence of metabolite
levels, and (iii) precision of measurements as a function of
concentration. These data provide more quantitative support
for the widely held notion that NMR metabolite measurements
are reproducible. Interestingly, a small number of metabolites
were found which do degrade significantly over time.
Poster 366
Metabolic Profiling and Investigation of Cellular Models of
Advanced Prostate Cancer
Christopher Mccullough; Niki Zacharias; Pratip Bhattacharya
M.D. Anderson Cancer Center, Houston, TX
There is an urgent need to better classify and treat prostate
cancer. Despite initial response rates of ~90% to androgendeprivation therapy among patients, most continue to develop
castration-resistant prostate cancer (CRPC). NMR can probe
1
cell metabolism changes in prostate cancer. Utilizing H-, J1
13
Resolved- H-, and C-NMR—while monitoring the uptake
and fate of specifically labeled precursors in feeding studies—
we metabolically profiled four human prostate cell lines,
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
ranging from indolent to aggressive cancer, including PC3M,
which serves as one CRPC model. Statistically significant
differences of several metabolites were found, suggesting a
potential mechanism of metastatic progression, motivating the
13
C-labeled compound feeding studies and further biological
assay characterization.
remove proton decoupling artifacts in 13C NMR of polyolefins,
10 mm high temperature cryoprobe which brought a revolution
to NMR characterization of polyolefins in chemical industry,
unsaturation measurements of polyolefins with the high
temperature cryoprobe and temperature gradient NMR for
characterizing polyolefins will be presented.
MATERIALS AND INORGANICS
367 - 421
Poster 370
Challenges and Solutions to the Chain End
Characterization of High Molecular Weight Polyolefins by
NMR
Yiyong He
The Dow Chemical Company, Midland, MI
Understanding the chain ends of polyolefins is important in
many respects. However, there are both technical and
scientific challenges. “Unexpected” proton T1s are reported for
the
solutions
of
poly(ethylene-co-1-octene)
and
tetrachloroethane-d2. Scientifically, the long standing
challenge is the differentiation and quantification of terminal
and internal unsaturated structures. To circumvent the
complication of T1 and minimize thermal degradation,
Cr(acac) 3 was added. Systematic work was done to study the
1
Cr(AcAc) 3 effect on H T1 and spectrum quality. The optimum
Cr(AcAc) 3 concentration was found to be 0.001 M. We
provided a robust and efficient procedure for characterizing
parts-per-million level chain ends in polyolefins, and
developed a new method to differentiate and quantify, for the
first time, terminal and internal unsaturations in ethylene-co-1octene copolymers.
Poster 367
Increasing the Range of Application of Size Exclusion
Chromatographic NMR
Guillermo Lucena; Iain Day
University of Sussex, Brighton, UK
In most analytical processes a huge quantity of resources are
employed to separate and purify both intermediate and final
compounds for their analysis. Thus, analytical methods of
mixtures are required to reduce time and efforts invested in all
this procedures.
Nuclear magnetic resonance is one of the most powerful
analytical techniques. Therefore, to improve the analysis of
mixtures, DOSY experiments have been combined with the
use of stationary phases or solvent additives that modify
diffusion properties to create chromatographic NMR. These
ideas have been extended to size exclusion stationary phases
and demonstrated their use on a range of polymers. Our aim
here is to extend the use of SEC-DOSY to a wide range of
systems including inorganic complexes and proteins.
Poster 368
Towards Understanding Switchable Dielectric Response
in Perovskite-Type Metal−Organic Framework (MOF)
Materials: A Solid State NMR Approach
Yefeng Yao
East China Normal University, Shanghai, China
In this work, we studied two Perovskite-type MOF materials
([(CH3) 2NH2] 2-[KCo-(CN) 6] and (Im) 2-[KCo(CN) 6], Im =
imidazolium), which both have a marked switchable dielectric
1
2
13
transition. Through combination of solid state H, H, C
NMR, we probed the motions of the caged molecules in the
materials. The obtained information about the motions of the
caged molecules (i.e., frequency and geometry) provide
possible molecular mechanisms of the dielectric transitions of
the materials.
Poster 369
New NMR Techniques Developed Recently for Studying
Polyolefin Microstructures
1
2
3
1
1
Zhe Zhou ; R Kuemmerle ; D Mekap ; D Redwine ; R Cong ;
3
3
1
1
1
1
F Malz ; R Brüll ; J.C. Stevens ; J Klosin ; S Qiu ; Y He ; W
1
1
1
1
DeGroot ; B Winniford ; M Miller ; P Chauvel
1
2
The Dow Chemical Company, Freeport, TX; Bruker Biospin
AG, Zurich, Switzerland;
3
Fraunhofer Institute, Darmstadt, Germany
Polyolefins, with their excellent cost/performance ratio, are by
volume the most produced synthetic polymers with a global
production of 147 million tons in 2011 and a predicted growth
to 170 million tons by 2017. Understanding polyolefin
molecular structure and property relationships are a key to
improve catalyst systems and process technologies. NMR is
one of the best techniques to achieve this goal. New NMR
techniques developed recently, such as bi-level decoupling to
Poster 371
Doubling Sensitivity in Solids NMR : A Simple and
Economical Procedure for Compressing Samples
Andre J Simpson; Ioana Fugariu; Blythe Fortier-McGill;
Ronald Soong; Andre Sutrisno
University of Toronto, Toronto, Canada
Here a simple and cost effective approach that doubles the
sensitivity and consequently gives a fourfold reduction in
measurement time for most samples is presented.
Specifically, the advantages of externally preparing vitrified
pellets under ultra-high (10 tons) pressures for CP-MAS NMR
are demonstrated. The ultra-high pressure packing system
employs a readily available commercial stainless steel dry
pressing die set, which produces a circular compressed sheet,
from which smaller pellets are extracted using a hollow punch
(3.2 mm ID). Typically six to seven pellets are required to fill a
rotor, resulting in rotors with approximately double the mass
compared to those that are packed regularly, which could
potentially allow otherwise inaccessible experiments to be
performed.
Poster 372
Multiple Water and Proton Environments in Swollen
Nafion: Insight into Proton Transfer
Mechanism in Fuel Cells
1
1, 2
Hyun Na Kim ; Oc Hee Han
1
Korea Basic Science Institute, Seoul, Republic of Korea;
2
Graduate School of Analytical Science and Technol,
Daejeon, Republic of Korea
The proton transport mechanism in hydrated Nafion for a
polymer electrolyte membrane fuel cell, has been extensively
investigated for decades to enhance the efficiency of fuel
cells. In this work, we report the multiple proton sites in Nafion
1
2
swollen in H2O or D2O after heat-treatment using H and H
Page 109
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
MAS NMR spectroscopy. Our results suggest that the
formation of closed hydrophilic channels upon heat-treatment
of Nafion, where the fast-exchange of protons between water
and sulfonic acid groups is inhibited. The formation of closed
hydrophilic channels may hinder efficient proton transport in
fuel cells. Dynamic behavior of protons at different sites and
various hydration levels were also investigated, which is
expected to enhance our understanding of proton transport
mechanism.
Poster 373
A Cryogenic NMR Study on Superconducting
Endohedral Fullerides
1
2
2
Richard Bounds ; Ivo Heinmaa ; Raivo Stern ; Mark
1
3
1
Denning ; Yasujiro Murata ; Andrea Krachmalnicoff ; Richard
1
1
Whitby ; Marina Carravetta
1
2
University Of Southampton, Southampton, UK; National
3
Institute of Chemical Physics, Tallin, Estonia; Kyoto
University, Kyoto, Japan
Recent success in synthetic methods for the encapsulation of
H2O and H2 molecules inside C60 have instigated a wide
range of studies on the endohedral fullerenes, but not
endohedral fullerides. Samples of superconducting Rb3C60
with H2O or H2 molecules inside the fullerene cage have been
synthesised for the first time by our group. We report here the
characterization of these materials and also a study on the
superconducting properties, investigated using NMR
techniques as a function of temperature. Our objective was
the study of how the dipole moment of water affects
superconductivity, which we compare with H2@C60 and
1
13
normal C60. Static H and C NMR data at 4.7 T and 8.5 T in
the normal and superconducting state is presented.
Poster 374
Long-range Lithium Ion Diffusion in a Garnet-Type Solid
Conductor Li7La3Zr2O12 Studied by PGSE-NMR Method
1
2
Kikuko Hayamizu ; Shiro Seki
1
2
University of Tsukuba, Tsukuba, Japan; Central Research
Institute, Tokyo, Japan
Lithium ion solid conductors are known to have high ionic
conductivity, which conduction is produced by lithium ion
diffusion. Garnet-type solid conductors have been studied
6,7
Li relaxation times. We have reported that
precisely by
lithium ion diffusion in sulfide-type conductors (Li2S) n (P2S5) 17
n by PGSE- Li-NMR are found the phenomena are very
unique. The lithium diffusion depends on measuring
parameters such as observation time (Δ) and PFG strength g.
Also, the diffusion plots showed diffractive patterns when Δ
was short and very long. In this study we observed the lithium
diffusion in garnet-type Li7La3Zr2O12 (LLZO) in fine crystals.
We found the relationships between grain boundary and the
diffractive patterns in the echo attenuation plots
Poster 375
NMR Study of Ion Dynamics and Charge Storage in Ionic
Liquid Supercapacitors
1
1
1
Alexander C. Forse ; John M. Griffin ; Céline Merlet ; Paul M.
1
1
2
2
Bayley ; Hao Wang ; Daniel Weingarth ; Volker Presser ;
3
4
1
Yury Gogotsi ; Patrice Simon ; Clare P. Grey
1
2
University of Cambridge, Cambridge, UK; Leibniz-Institute
3
for New Materials, Saarbrücken, Germany; Drexel University,
4
Philadelphia, PA; Université Paul Sabatier, Toulouse, France
Supercapacitors are high power energy storage devices that
store charge in electric double-layers at the interface between
Page 110
an ionic solution and porous carbon electrodes. We have
developed NMR methods to study the composition and
dynamics of the electric double-layer in these important
devices. The chemical shifts observed for adsorbed ions are
sensitive to the local structure of carbon surfaces, while
lineshapes provide information on ion dynamics. This has
allowed us to compare different ionic liquids and carbons and
explain their performance in supercapacitors. Finally, NMR
experiments on electrodes with different applied voltages
reveal that supercapacitor charging is achieved by exchange
of anions and cations in and out of the carbon pores.
Poster 376
Exploiting Chemical Shift Anisotropy in
Liquid Crystal Thermosets
1
2
1
Leah M. Heist ; Theo J. Dingemans ; Edward T. Samulski
1
2
UNC Chapel Hill, Chapel Hill, NC; Delft University of
Technology, Delft, Netherlands
We use ultra-high temperature, 13C NMR to monitor
thermally-induced curing in liquid crystal thermosets (LCTs), a
new class of high performance polymers. LCTs utilize reactive
phenylethynyl end-capped oligomers that have desirable
processing characteristics as the reactive end-group
effectively slows down radical formation delaying cross-linking
until temperatures exceed 300°C.
In order to understand the curing, e.g. the kinetics and final
products formed, we constructed a high temperature NMR
probe (>400°C) capable of reaching LCT curing temperatures.
In the nematic melt, the LCT director spontaneously aligns
along the spectrometer magnetic field identifying the reactive
acetylene group by its distinct chemical shift anisotropy
(CSA). NMR spectra at different curing temperatures and
times yields information about the cure kinetics.
Poster 377
Sealed Rotors for in situ MAS NMR
Jian Zhi Hu; Mary Hu; Zhenchao Zhao; Suochang Xu; Hui
Shi; Aleksei Vjunov; Donald M Camaioni; Johannes A.
Lercher; Charles H. F. Peden
Pacific Northwest National Laboratory, Richland, WA
We report the progress of developing a perfectly sealed MAS
rotor for all kinds of in situ MAS NMR experiments where
samples need be sealed from exposing to surrounding
environments. The MAS rotor with all parts made of high
mechanical strength ceramics such as zircornia except an Oring and a spin-tip, is easy to operate and reusable for
hundreds of times without performance degradation. The
rotor is potentially capable of simultaneous high pressure
operation in excess of 100 bars and temperature in excess of
250 ºC. This capability is an idea tool for quantitatively
investigating the reaction dynamics and pathways associated
with catalytic reactions and materials synthesis. Application
examples will be presented.
Poster 378
Low Field EPR in Cultural Heritage Science; The Nondestructive Characterization of Large Intact Objects and
Spin Dynamics at Low Frequncies
1
2
Nicholas Zumbulyadis ; Lauren Switala ;
2
2
William Ryan ; Joseph Hornak
1
2
Independent Researcher, Rochester, NY; Rochester
Institute of Technology, Rochester, NY
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
We report our recent work in the use of Low-Field EPR
(LFEPR) as a non-destructive/non-invasive technique for
studying ceramic or marble cultural heritage objects. We have
examined intact objects over ten centimeters using 250 MHz
LFEPR. None of these objects fits in a conventional EPR
spectrometer and previously would have required invasive
sample removal. The spectra of ceramics show features of
S=5/2 Fe(III) displaying a g≈4 peak (Fe(III) substituting for Al
in aluminosilicate lattices), a g≈2 peak (Fe(III) in iron oxide) or
orientation-dependent ferromagnetic resonance behavior. We
have also studied Mn(II) in marble. The LFEPR spectrum
differs significantly from the classical Mn(II) high field EPR
spectrum. The high field approximation breaks down when the
Zeeman and hyperfine interactions become comparable.
Poster 379
Three-Dimensional Structure Determination of Surface
Species by DNP Enhanced Solid-state NMR
1
1
1
Pierrick Berruyer ; Moreno Lelli ; Alexandre Zagdoun ; David
1
2
4
3
Gajan ; Aaron J. Rossini ; Matthew Conley ; Olivier Ouari ;
3
4
Paul Tordo ; Christophe Copéret ;
1
1, 2
Anne Lesage ; Lyndon Emsley
1
2
Ecole Normale Supérieure, Lyon, France; Ecole
3
Polytechnique Fédérale, Lausanne, CH; Aix-Marseille
4
University, Marseille, FR; ETH, Zürich, CH
Because it provides dramatic sensitivity enhancement, solidstate Dynamic Nuclear Polarization (DNP) NMR is currently
emerging as a powerful tool to study samples previously
inaccessible to NMR. We have recently shown how DNP
could be used to selectively enhance the NMR signals from
surfaces in a wide range of samples, including nanoporous
and nanoparticulate materials (DNP SENS).Here we will show
that DNP SENS in combination with multi-nuclear correlation
techniques can be applied to obtain quantitative
measurements of 13C-15N and 29Si-15N distances in
mesoporous silicas incorporating organic fragments as well as
well-defined organometalic catalysts leading to the
determination of the three-dimensional structure of the surface
species for both precursor and metal-organic catalyst.
Poster 380
In situ High Temperature High Pressure MAS NMR Study
on the Crystallization of AlPO4-5
1
1
1
Zhenchao Zhao ; Suochang Xu ; Mary Hu ;
2
1
Xinhe Bao ; Jian Zhi Hu
1
2
Pacific Northwest National Laboratory, Richland, WA; Dalian
Institute of Chemical Physics, Dalian, China
Unraveling the crystallization mechanism of molecular sieves
is of great interest in engineering designable synthesis of
molecular sieves and fundamental science. Herein, we report
in situ multinuclear 27Al, 31P, 13C, 1H and 13C CP/MAS
NMR investigations of the crystallization process of AlPO4-5
molecular sieve. The roles of water and significant changes
during induction period for nucleation are demonstrated for
the first time. A crystallization model, i.e., the continuous
rearrangement of the local structure from amorphous gel
aided by active water during heating and induction period to
form crystal AlPO4-5, is proposed.
Poster 381
Investigation of Aluminum Site Changes of Dehydrated HBeta during a Rehydration Process by High Field Solid
State NMR
1
1
1
2
Zhenchao Zhao ; Suochang Xu ; Mary Hu ; Xinhe Bao ;
1
1
Charles H.F. Peden ; Jian Zhi Hu
1
2
Pacific Northwest National Laboratory, Richland, WA; Dalian
Institute of Chemical Physics, Dalian, China
Aluminum sites in zeolites are directly associated with the
active center―Brönsted and Lewis acid sites when zeolites
are used as catalysts. The activated zeolite catalysts are often
in H-form and dehydrated state, and thus 27Al MAS NMR
investigation of dehydrated zeolite is of great interest but with
great challenge due to extremely strong quadrupole
interactions. Here, we report quantitative 27Al MAS and MQ
MAS NMR investigations probing aluminum site changes of
fully dehydrated H-Beta zeolite during a progressive water
adsorption processes at high magnetic fields up to 19.97 T.
Extra-framework aluminum sites increase initially as some
invisible aluminum species change into the penta- and
octahedrally coordinated aluminum, and finally disappear by
changing into tetra-coordinated framework/extra-framework
aluminums during the rehydration process.
Poster 382
Investigation of Diffusion Complexities in Heterogeneous
Systems with NMR Diffusion Tensor Imaging
Shangwu Ding
National Sun Yat-Sen University, Kaohsiung, Taiwan
The diffusion complexities in heterogeneous materials
abound, such as surface effect, anomalous diffusion, which
bring additional challenge to quantitative description of
diffusion in this type of materials. We show that NMR diffusion
tensor imaging (DTI), combined with a novel statistical
method, can be employed to characterize these complexities.
The method is demonstrated with Nafion (proton exchange
membrane for fuel cells). It is found that the single exponential
model currently used in DTI must be modified to describe
diffusion in each pixel more accurately. The new complexties
revealed by our method provide better understanding of the
structure and dynamics of heterogeneous materials. This new
analysis method for DTI can be immediately used in medical
and functional imaging.
Poster 383
Interface-Selective NMR of Macromolecules in Contact
with Solid Substrates
Ulrich Scheler
Leibniz-Institut Für Polymerforschung Dresden E.V.,
Dresden, Germany
Macromolecules, proteins or polymers, in contact with
inorganic materials appear in nature like bone or in polymer
materials. The interface between the organic and the
inorganic phase determines the properties. Different
approaches have been used for the selective excitation of the
19
interface. Sensitive nuclei in the inorganic matrix like F or
31
P can be used as source of magnetization for transfer via
cross polarization or multiquantum, the OH signal in
hydroxyapatite is selected by a combination of chemical-shift
and T2 selection. Subsequent proton spin diffusion carries the
magnetization in the interface region. Placing spinlabeled
polyelectrolytes on the interface enables DNP based solidstate NMR.In any case subsequent spin diffusion caries
magnetization into the organic phase for spectroscopy or
relaxation studies.
Page 111
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
Poster 384
Hyperpolarized para-ethanol
1
1
1
Daniele Mammoli ; Basile Vuichoud ; Aurélien Bornet ; Jonas
1
2
1
Milani ; Jean-Nicolas Dumez ; Sami Jannin ; Geoffrey
1, 3
Bodenhausen
1
EPFL, École polytechnique fédérale de Lausanne, Lausanne,
2
Switzerland; CNRS, Centre national de la recherche
3
scientifique, Gif-sur-Yvette, France; ENS, École Normale
Supérieure, Paris, France
In our work we show that it is possible to use Dissolution
Dynamic Nuclear Polarization (D-DNP) to create a tripletsinglet (T/S) imbalance in the pair of magnetically equivalent
13
protons of partly deuterated ethanol (CD3 CH2OD) and
observe it without chemical reactions by monitoring its cross1
13
relaxation into observable transitions of either H or C nuclei.
13
1
We found antiphase doublets of the C satellites in the H
13
spectra and non-binomial triplets in the C spectra.
Simulations with
mechanism.
SpinDynamica
confirm
the
proposed
This experimental scheme should be widely applicable to
13
virtually to any molecule containing a CH2 group.
Poster 385
Two-Dimensional NMR Measurement and Point Dipole
Model Prediction of Paramagnetic Shift Tensors in Solids
1
2
3
Brennan Walder ; Krishna Dey ; Michael Davis ; Jay H
4
1
Baltisberger ; Philip Grandinetti
1
2
The Ohio State University, Columbus, OH; Dr. H.S. Gour
3
University, Sagar, MP, India; Bridgestone Americas Center
4
for Research and Tech., Akron, OH; Berea College, Berea,
KY
We have analyzed various methods for separating and
correlating the paramagnetic shift and quadrupolar coupling
frequency contributions in polycrystalline samples. On the
basis of our analysis we propose a sequence that suppresses
the spectral distortions of the pre-existing methods while
improving sensitivity. We illustrate our approach on a sample
2
of CuCl2 • 2D2O. A simple model for the H efg tensor
orientation accurately predicts the observed quadrupolar
2
coupling. A nuclei-centered point dipole model predicts a H
paramagnetic shift tensor in poor agreement with our
measured values. This is rectified when the point dipoles are
displaced away from the nuclei at positions consistent with the
maximum electron density of the lobes of the singly occupied
anti-bonding molecular orbital.
Poster 386
Solid-State Dynamics and Hydrogen Bonding in Uranyl
Clusters using Multi-Nuclear MAS NMR Spectroscopy
1
2
2
3
Todd M. Alam ; May Nyman ; Zuolei Liao ; Jonathan Yates
1
2
Sandia National Laboratories, Albuquerque, NM; Oregon
State University, Corvallis, OR;
3
University of Oxford, Oxford, UK
1
23
7
1
23
Multi-nuclear ( H, Na and Li) MAS NMR and 2D H- Na
1
7
and H- Li HETCOR MAS NMR correlation experiments
1
combined with 2D H DQ and NOESY NMR correlation
experiments have been used to investigate the solid state
exchange dynamics and structural location of the cations in a
series of uranyl-polyoxometalate (POM) U24 clusters.
+
+
Surprisingly it is shown that there is rapid Li and Na cation
exchange from environments inside the uranyl cluster
(encapsulated) to outside (lattice) occurring on the milliPage 112
second time scale near room temperature even in the solid
state. Details about the different proton environments were
obtained from developed correlations between hydrogen bond
1
strength and the H NMR chemical shifts for uranyl hydroxyls
based on CASTEP GIPAW chemical shift simulations.
Poster 387
3+
Characterization of Ln -doped Nanoparticles Using
Solid-State NMR
1
1
2
David A. Hirsh ; Bryan E.G. Lucier ; Anna M. Ritcey ; Robert
1
W. Schurko
1
2
University of Windsor, Windsor, Canada; Université Laval,
Québec, Canada
Inorganic nanoparticles (NPs) containing lanthanide(III)dopants have desirable optical properties (e.g., long
luminescence lifetimes) that make them ideal for use in LEDs,
lasers, and imaging. As these properties are highly sensitive
to the local structure around the dopant ions, characterization
of such NPs on a molecular level is vital to improve their
rational design and preparation. Herein, we present a
+
multinuclear SSNMR study of zeolitic (H3O )Y3F10•xH2O NPs
that contain rare-earth dopants. These experiments reveal
the core NP structures (and their similarities/differences with
the undoped material) as well as the dopant positions and
uniformity within the NP. Our findings will aid in the design
and synthesis of advanced rare-earth NPs with fine-tuned
optical properties.
Poster 388
33
High-resolution S MAS NMR at Natural Abundance:
Application to the Cement Mineral Ettringite
Stephen Wimperis; Akiko Sasaki
University of Glasgow, Glasgow, UK
Despite the wide prevalence of sulfur in materials science,
33
there have been very few S (I = 3/2) solid-state NMR studies
owing to the low natural abundance (0.76%), low
gyromagnetic ratio (30.7 MHz at B0 = 9.4 T), and the high cost
33
of S enrichment. Here, we demonstrate the feasibility of
33
natural abundance S STMAS at B0 = 20.0 T using a model
system (1:1 molar mixture of Na2SO4 and K2SO4) and then
33
apply the high-resolution S STMAS method at B0 = 9.4 T
and 20.0 T in an attempt to resolve and characterise the
distinct S sites in ettringite (Ca6Al2 (SO4) 3 (OH) 12·26H2O), a
mineral that is important in the chemistry of concrete and
cement.
Poster 389
Characterization of Bonding Preferences in Ca/Na and
Ca/F Aluminosilicate Glasses using Solid-State J-based
MAS NMR technics
Pierre Florian
CEMHTI-CNRS, Orleans Cedex 2, France
Here we applied high magnetic field (20.0 T) to reduce the
27
17
effects of quadrupolar interaction and measure J ( Al, O)
23
17
and J ( Na, O) scalar couplings in the solid-state. This
17
allows us to filter the
O MAS NMR signal using
heteronuclear J-based sequences making it possible to
characterize calcium and sodium environments in CaOAl2O3-SiO2 (CAS) and CaO-Na2O-Al2O3-SiO2 (CNAS) glass
27
17
23
17
by { Al} O and { Na} O MAS INEPT technics. Those data
show that calcium ions are preferentially located nearby the
SiO4 units whereas sodium ions mainly behave as charge
compensator of the AlO4 species. When applied to fluorinecontaining CAS, this J-based methodology shows also
POSTERS
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
preferential bonding of the fluorine atom towards specific
aluminum building units.
Poster 390
Monitoring the Formation of a Zeolitic Imidazolate
Framework Using Multinuclear Solid-State NMR
1
2
2
Christopher O'keefe ; Cristina Mottillo ; Tomislav Friščić ;
1
Robert Schurko
1
University of Windsor, Windsor, Canada;
2
McGill University, Montréal, Canada
Mechanochemistry and accelerated aging are two synthetic
approaches that are consistent with the philosophy of green
chemistry. Recently, these approaches have been applied to
the synthesis of zeolitic imidazolate frameworks (ZIFs), which
are of interest due to their uses in catalysis and gas storage.
The mechanisms and factors affecting ZIF synthesis are
largely unknown. Recent mechanistic studies utilized X-ray
diffraction (XRD) experiments to identify product and
intermediate phases; however, the elucidation of the structure
of the amorphous intermediate phases was not possible.
111
1
13
Herein, we describe the use of multinuclear ( Cd, H, C
14
and N) SSNMR to characterize the product and intermediate
phases, as well as to monitor the formation of the Cd[2methylimidazole] 2 ZIF which is formed using both synthetic
approaches.
reported solid-state NMR data of these materials whose gas
adsorption properties are often poorly studied at the molecular
level.
Poster 393
Solution Phase Strategies for Metal Nanoparticle Growth
on Colloidal Plasmonic Substrates
Jill Millstone; Patrick Straney; Lauren Marbella
University of Pittsburgh, Pittsburgh, PA
Small molecule ligand chemistry is used to mediate the
incorporation and distribution of metals in and on discrete,
colloidal nanoparticle substrates. We examine the case of Au
195
and Pt, and monitor the impact of Pt chemistry via Pt NMR.
The results provide important mechanistic platforms for the
development of nanoscale platinum materials, used across a
wide variety of heterogeneous catalytic reactions important in
the generation of solar fuels and industrial fossil fuel
1
conversion. Further, we use H NMR to highlight the role of
substrate surface chemistry in the morphology of the resulting
mixed metal nanoparticles, and show that surface ligand
supramolecular assembly may be a promising new tool in the
development of on-colloid lithographies and nanoparticle selfassembly strategies.
Poster 391
Gold-Cobalt Nanoparticle Alloys Exhibiting Tunable
Compositions, Near-Infrared Emission, and High T2
Relaxivity
Lauren Marbella; Christopher Andolina;
Ashley Smith; Jill Millstone
University of Pittsburgh, Pittsburgh, PA
We demonstrate the synthesis of composition-tunable goldcobalt nanoparticle alloys (% Co = 0–100%; d = 2–3 nm), in
contrast with bulk behavior, which shows immiscibility of Au
and Co at room temperature across all composition space.
These particles are characterized by transmission electron
1
microscopy and H NMR, as well as ICP-MS, XPS, and
1
photoluminescence spectroscopy. In particular, H NMR
methods allow the simultaneous evaluation of magnetic
properties as well as molecular characterization of the colloid,
including ligand environment and size. We also identify
AuxCoyNP compositions that exhibit both bright NIR emission
−1
−1
(2884 M cm ) as well as some of the highest per-particle T2
−1 −1
relaxivities (12200 mMNP s ) reported to date for this particle
size range.
Poster 394
Solid-state NMR Characterization of Quadrupolar Nuclei
in Metal-oxide Clusters
1
1
1
Blake Hammann ; Zayd Ma ; Katherine Wentz ; Maisha
2
3
Kamunde-Devonish ; Victor V. Terskikh ; Darren W.
2
1
Johnson ; Sophia E. Hayes
1
2
Washington University, St. Louis, MO; University of Oregon,
3
Eugene, OR; University of Ottawa, Ottawa, ON
Metal-oxide clusters have become a popular subject matter in
solid-state NMR due to the advancements in high magnetic
fields and ultra-fast MAS probes. These clusters often contain
quadrupolar nuclei (such as aluminum or gallium, nuclear spin
I=5/2 and 3/2, respectively), which can present a substantial
challenge in acquiring high resolution NMR spectra. However,
the quadrupole coupling to the electric field gradient can yield
a wealth of structural information. We present a study on
group 13 metal-oxide clusters that contain hydroxo-bridged
ligands and have a structural formula of [M13-xInx (μ3-OH) 6 (μ2OH) 18 (H2O) 24](NO3) 15 (M = Al, Ga). Monitoring the
coordination environment and characterizing the metal sites
allows for important structural information to be gained on
understanding the transformation of the cluster precursors to
thin films.
Poster 392
Understanding the Gas Adsorption Properties in MetalOrganic Frameworks by Solid-State NMR
Jun Xu
UC Berkeley, El Cerrito, CA
As an important class of porous materials, metal-organic
frameworks (MOFs) have been shown to be suitable for the
application as gas adsorption and separation materials. MOF74 or related MOFs are promising candidates for this
application due to the open metal centers. Unfortunately the
adsorption properties of these MOFs decreases under humid
environments since open metal centers also have high affinity
to water. Several approaches have been proposed to develop
new MOF-74 based materials that are more tolerant of humid
conditions including appending alkyldiamines inside of MOF
channels and preparing mixed metal MOF-74. In this work, we
Poster 395
Instrumentation of in-situ Gas Loading Apparatus for
Magnetic Resonance Gas Diffusion Studies in
Metal Organic Frameworks
Velencia Witherspoon; Martin Gelenter;
Lucy Meng Yu; Jeffrey Reimer
UC Berkeley, Chemical Engineering, Berkeley, CA
A novel class of porous media are metal-organic frameworks
(MOFs) composed of a crystalline network of metal clusters
coordinately bonded to organic linkers. These materials
posses potential for gas separations because of their large
surface areas, high selectivity, and tunable pore size and
surface chemistry. In order to better assess and intellectually
direct the design of these materials, an in situ apparatus for
gas loading was constructed for use in gas diffusion and
relaxation measurements. The diffusion and relaxation of CH4
Page 113
POSTERS
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
and CO2 were measured in IRMOF-1 and IRMOF-3 at various
loadings and temperatures. Some molecular dynamic
simulations were performed to model the results.
Poster 396
Surface-Enhanced DNP-CPMAS Studies of Adsorbed
Organic Monolayers on Low-Surface-Area
Silicate Particles
1
2
2
Rahul P. Sangodkar ; Aaron J. Rossini ; David Gajan ;
3
4
2
Lawrence R. Roberts ; Gary P. Funkhouser ; Anne Lesage ;
2, 5
1
Lyndon Emsley ; Brad Chmelka
1
University of California Santa Barbara, Santa Barbara, CA;
2
3
CRMN Lyon/ENS Lyon, Lyon, France; Roberts Consulting
4
5
Group, Acton, MA; Halliburton, Houston, TX; EPFL,
Lausanne, Switzerland
Solid-state dynamic nuclear polarization (DNP) NMR
techniques with cross-polarization magic-angle-spinning
(CPMAS) are used to elucidate the competitive adsorption of
industrially relevant dilute organic molecules at inorganic
13
1
29
1
31
1
29
13
surfaces. Solid-state C{ H}, Si{ H}, P{ H}, Si{ C} DNPNMR measurements, including rotational echo double
resonance (REDOR) and two-dimensional (2D) heteronuclear
correlation (HETCOR), are reported for
low absolute
concentrations (~0.1 wt%) of saccharide and phosphonic acid
2
molecules adsorbed at low-surface-area (~1 m /g) silicate
particles. The DNP-enhanced signal sensitivity enables
detection of such dilute surface species that has until now
been infeasible and establishes that sucrose and phosphonic
acid inhibit hydration through physicochemically distinct
adsorption behaviors, which depend on their molecular
architectures. These molecular insights are directly related to
the macroscopic rheological and mechanical properties of
cement-water mixtures.
Poster 397
Chemisorption Reactions and Mineralization of CO2
13
Studied with C Solid-State NMR
Jeremy K. Moore; J. Andrew Surface; Mark S. Conradi;
Sophia E. Hayes
Washington University, St. Louis, MO
The rising concentration of CO2 in the atmosphere has
increased studies on the capture and sequestration of CO2.
Solid supported-amine adsorbents are reacted with CO2 and
13
have been monitored with in situ static C NMR which shows
13
1
that the amines chemisorb CO2. With C{ H} CPMAS NMR,
the chemisorbed product is identified as a mixture of
carbamate and bicarbonate. The captured CO2 can be
sequestered through geologic mineralization reactions in
2+
2+
which divalent cations (Fe , Mg , etc.) react with CO2 to form
metal carbonates. Magnesite (MgCO3) and meta-stable
magnesium carbonate minerals have been characterized via
their distinct chemical shift anisotropy (CSA) parameters with
13
static C MAS NMR.
Poster 398
NMR Crystallography of a Photo-Intermediate in the
Solid-State Crystal-to-Crystal Photoreaction of 9TBAE
1
1
1
1
Chen Yang ; Ryan Kudla ; Lingyan Zhu ; Jinfeng Lai ; Rabih
3
2
2
Al-Kaysi ; Stephen Monaco ; Bohdan Schatschneider ;
1
1
Christopher Bardeen ; Leonard Mueller
1
University of California Riverside, Riverside, CA;
2
3
Pennsylvania State University, Lemont Furnace, PA; KSAUHS&&KAIMRC, Ar Rimayah, Riyadh
Page 114
The photodimerization of 9-tertbutyl-anthracene ester
(9TBAE) in molecular crystal nanorods leads to expansions of
up to 15%, indicating a promising new paradigm for lightcontrolled actuators. The expansion results from the formation
of a metastable crystal intermediate, the solid-state reacted
dimer (SSRD). Here we combine powder X-ray diffraction
(PXRD), DFT calculations, and solid-state NMR to resolve the
structure of the transient SSRD. In this NMR crystallography
approach, PXRD produces potential crystal structures, DFT
calculations both refine the structure in the solid state and
provide computed chemical shieldings, and SSNMR chemical
shifts are used to screen and rank potential candidates.
Based on the crystal structure of SSRD, we proposed a novel
symmetry-breaking mechanism for the photoinduced
expansion.
Poster 399
Intermolecular Interactions of Hydrated β-Dicalcium
Silicate Particles Probed by Solid-State NMR
1
2
Scarlett Widgeon ; Mariane Silva de Miranda ; Flávio
2
1
Aparecido Rodrigues ; Bradley F. Chmelka
1
2
UC Santa Barbara, Santa Barbara, CA; Universidade de
Mogi das Cruzes, Mogi das Cruzes, Brazil
Solid-state MAS NMR techniques have been used to establish
the molecular compositions and structures of anhydrous βdicalcium silicate and to monitor changes that occur as a
result of hydration. Quantitative single-pulse 29Si MAS NMR
measurements are used to monitor the distinct molecular
changes and extents of hydration. Two-dimensional 29Si{1H}
heteronuclear correlation (HETCOR) NMR spectra reveal
different distributions and intermolecular interactions of silicate
species with water and hydroxyl moieties. Such molecularlevel insights are correlated with differential scanning
calorimetry measurements that show enthalpies of anhydrous
β-dicalcium silicate made by the two methods are different.
These results provide understanding of the underlying
processes that control the hydration rates of β-dicalcium
silicate which are expected to provide new criteria for
engineering anhydrous cement mixtures.
Poster 400
69,71
Ga NMR Evidence for Electron Carriers in
Solid-State
Annealed Gallium Nitride Nanoparticles
1
2
Zachariah Berkson ; James Yesinowski ;
1, 3
2
Sylvian Cadars ; Andrew Purdy ;
1, 4
1
Ulrike Werner-Zwanziger ; Bradley Chmelka
1
Department of Chemical Engineering, UCSB, Santa Barbara,
2
CA; Chemistry Division, Naval Research Laboratory,
3
Washington, DC; CEMHTI CNRS UPR3079, Université
4
d’Orléans, Orléans, France; Department of Chemistry,
Dalhousie University, Halifax, Canada
Using wide-line excitation and spectral editing techniques,
71
69
solid-state Ga and Ga NMR spectra and spin-lattice
relaxation time measurements elucidate differences among
local gallium environments in bulk gallium nitride (GaN) and hGaN nanoparticles. Broad distributions of disordered
environments in h-GaN nanoparticles, evidenced by solid71
69
state Ga and Ga NMR, are due to distributions of Knight
shifts arising from different extents of coupling among nuclear
and electron spins through hyperfine interactions. Saturation
recovery methods for quadrupolar nuclei are applied to
measure spin-lattice relaxation times, which agree well with
the theoretical Korringa expression that models spin-lattice
POSTERS
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
relaxation due to conduction electron coupling. Results
demonstrate that h-GaN nanoparticles can be prepared with
high charge carrier concentrations, with important implications
for electrical and optoelectronic semiconducting devices.
Poster 401
Assessing Fullerene Proximities to Donor and Acceptor
Moieties in Bulk Heterojunction Materials using SolidState NMR Spectroscopy
2
2
1, 3
Matthew Idso ; Justin Jahnke ; Kenneth Graham ; Aram
1
1
3
Amassian ; Pierre Beaujuge ; Michael McGehee ; Bradley
2
Chmelka
1
King Abdullah University of Science and Technology,
2
Thuwal, Saudi Arabia; University of California, Santa
3
Barbara, CA; Stanford University, Stanford, CA
Many highly efficient polymer:fullerene heterojunctions are
based on conjugated polymers that consist of distinct
electron-donor and electron-acceptor moieties and achieve
high charge-transfer efficiencies through the close molecular
proximities of polymer electron-accepting moieties and
13
1
C{ H}
fullerene species. Solid-state two-dimensional
heteronuclear correlation NMR techniques are used to
understand the molecular compositions, proximities, and
interactions in polymer:fullerene heterojunctions. Using these
methods, the close proximities of fullerene species with
polymer backbone moieties and straight alkyl sidechains are
established, demonstrating that polymer sidechain types (e.g.,
straight or branched) and architectures sterically influence the
relative arrangements of fullerene and polymer species.
These molecular insights into bulk heterojunctions are
correlated with macroscopic device performances to provide
criteria for the design of organic photovoltaic devices with
improved efficiencies.
Poster 402
Meso- and Nanopore Acidities in Mesostructured Zeolite
27
31
Beta Established by Solid-State 2D Al{ P} DNP-NMR
1
2
3
Matthew Aronson ; Yongbeom Seo ; Aaron J. Rossini ;
2
1
Ryong Ryoo ; Brad Chmelka
1
2
UCSB, Santa Barbara, CA; Korea Advanced Institute of
3
Science and Technology, Daejeon, South Korea; CRMN
Lyon/ENS Lyon, Lyon, France
Solid-state DNP-enhanced NMR provides unambiguous
information about the differences in acid-site strengths on
mesopore surfaces and within framework nanopores of
mesostructured zeolite Beta. More specifically, solid-state 2D
27
31
Al{ P} TEDOR DNP-NMR spectra reveal correlated signal
27
intensities associated with Al heteroatoms and adsorbed
31
trialkylphosphine oxide molecules, where the P chemical
shift is proportional to the Brønsted acid strength. The
27
27
observed Al signal intensities can be assigned to Al
moieties on the mesopore surfaces or within framework
31
nanopores, based on their correlations with P signals from
specific probe molecules, respectively. Measurements of
correlated signals from such species have previously been
infeasible by conventional solid-state NMR techniques due to
poor signal sensitivity, low concentrations of adsorbed
27
molecules, and rapid quadrupolar relaxation of Al spins.
Poster 403
Understanding Synthesis, Molecular Compositions, and
Conductivity of Nitrogen-Doped Carbon Materials with
13
15
Solid-State C and N NMR
1
2
2
Niels Zussblatt ; Nina Fechler ; Markus Antonietti ; Bradley
1
Chmelka
1
University of California, Santa Barbara, Santa Barbara, CA;
2
Max Planck Institute of Colloids and Interfaces, Potsdam,
Germany
High nitrogen content (28 wt%) carbonaceous materials were
synthesized and characterized by solid-state NMR
13
15
13
15
techniques, including C and N single-pluse, and C{ N}
13
15
REDOR. Quantitative ex situ C and N MAS NMR
measurements conducted to monitor formation of the Ncontaining aromatic network provided molecular-level
understanding of the synthesis process, nitrogenous moieties,
15
and that the N nuclei unusually serve as n-type dopants in
conjugated network.
REDOR NMR measurements
13
established that C nuclei are molecularly proximate (<1 nm)
15
to N nuclei, and that the material is composed of a multiply13
15
coupled spin pairs, rather than isolated C- N moieties.
Presence of pyridinic and pyrazinic moieties identified by
NMR characterization were found to be correlated with
macroscopic electrocatalytic oxygen reduction activity.
Poster 404
The Effect of Filler Dispersion and Molecular Dynamics
on Rolling Resistance of Silica Compounded Rubber
1
2
2
Kimiya Murakami ; Yoshihisa Inoue ; Takaaki Matsuda ;
1
1
Satoru Yamazaki ; Yasuhiro Hashimoto
1
2
Asahi Kasei Corporation, Fuji City, Japan; Asahi Kasei
Chemicals Corporation, Kanagawa, Japan
With growing concerns in global warming and increase of
CO2, the low fuel consumption tire attracts attentions in the
automotive industry, where silica compounded rubber is
increasingly used to reduce the tire rolling resistance (RR).
Since the importance of the uniformity of silica particle
distribution has been well understood, either functionalized
rubber or silane coupling agent is used to alleviate the silica
particle aggregations. Thus we conducted researches to
understand comprehensively the RR reduction mechanism in
terms of 1) the silica particle distribution, 2) the polymer
dynamics and 3) the related reaction between rubber,
coupling agent and silica. Here in this contribution, our recent
solid state and pulsed NMR results will be presented.
Poster 405
Understanding of Morphology Degradation of Nafion with
Solid State NMR Spectroscopy and Micro-Imaging
Ren-Hao Cheng; Cheng-Yu Shi; Shangwu Ding
Natl Sun Yat-sen Univer, Kaohsiung, Taiwan, Province of
China
In this work, we propose and demonstrate a method based on
solid state NMR spectroscopy and micro-imaging,
supplemented with XRD, SEM, TEM and theoretical modeling.
to quantify the morphology degradation of proton exchange
membrane Nafion, a longstanding problem owing its multiscale spatiotemporal complexities. Compared to the slight
changes of spectral characteristics, changes in relaxation and
diffusion rates across the sample are much more appreciable.
The possible mechanisms and consequences of morphology
degradation are analyzed and the implications to PEM
durability are discussed.
Page 115
POSTERS
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Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
Poster 406
Very Low Temperatures NMR (VLT NMR) Facility for
Transuranium Compounds at JRC-ITU
1
2
1
Laura Martel ; Yo Tokunaga ; Chris Selfslag ; Francois
1
1
Kinnart ; Jean Christophe Griveau
1
2
JRC-ITU, Eggenstein Leopoldshafen, Germany; ASRC,
Japan Atomic Energy Agency, Tokai, Ibaraki, Japan
Here, we present our recent developments made for VLT
NMR in transuranic compounds using two different NMR setup. The first one is a LT Bruker cryostat to which absolute
filters were added coupled with an NMR probe and using a
9.4T Bruker spectrometer. The first results on NpAl2 will be
shown.
The main drawback to this set-up is a limitation at 20 K while
magnetic or superconducting transitions are often observed
below this temperature. To overcome this problem, a built-inhouse static NMR probe has been developed and coupled
with a PPMS magnet (field sweeping up to 14 T and T down
17
to 2 K). The first results on a liquid reference, H2 O, and the
17
mixed oxide U0.15Np0.85 O2 will be show.
Poster 407
Proton Detected HETCOR for Disordered Solids
1
1
1
Stephen K. Davidowski ; Samrat A. Amin ; Brian Cherry ;
2
1
Gregory P. Holland ; Jeffery L Yarger
1
2
Arizona State University, Tempe, AZ; San Diego State
University, San Diego, CA
The use of proton detection in multidimensional pulse
sequences has become omnipresent in liquid state NMR, but
has been used much less for solid-state NMR. This is mostly
due to broad signals from strongly dipole coupled-protons in
most solids negating the added sensitivity expected from
transferring magnetization to proton prior to detection.
However, in situations where the proton’s dipole couplings are
partially averaged due to dynamics or if the X-nuclei are
sufficiently broadened, a sensitivity advantage can be
observed. In the work presented, we show some examples
that make use of a proton detected heteronuclear correlation
(HETCOR) pulse sequence that offers a significant advantage
when analyzing a range of different disordered materials,
including spider silk biopolymers, nanomaterials, and
synthetic polymers.
Poster 408
Phase Conversion of COF-1 in the Presence of
Mesitylene: Kinetic and Mechanistic Study
Kanmi Mao; Yi Du; Peter Ravikovitch; Bradley Wooler; David
Calabro
ExxonMobil, Clinton, NJ
Covalent Organic Frameworks-1 (COF-1) is a 2D porous
crystalline material with potential applications in gas
separation and storage. The as-synthesized COF-1 exists in
an AB staggered phase and will convert to AA eclipsed phase
after activation. This irreversible phase conversion have been
studied using solid-state NMR, in situ X-ray diffraction, and
1
1
Molecular Dynamics simulations. H- H double quantum
magical angle spinning demonstrates the close proximity
between mesitylene and frameworks in the presence of hostguest interactions. The activation energy for phase changing
reaction has been measured by in situ XRD. Theoretical
calculation suggests that mesitylene-framworks interaction
stabilizes AB configuration because COF-1 pore diameter and
the mesitylene molecule are comparable in size. This study
Page 116
provides useful guidance for topology design by revealing
solvent-framework interactions.
Poster 409
Effect of Fluorine on the Structure of
Fluorohydroxyapatite: A Solid State NMR Study
Peizhi Zhu
Yangzhou University, Yangzhou, China
A series of fluorohydroxyapatites were synthesised and
characterized to evaluate the effects of fluorine on the
structure of hydroxyapatite. For the first time we observed the
well-resolved Ca(I) and Ca(II) signal change in
fluorohydroxylapatite with different fluorine contents at nature
abundance. Compared with small variations of 31P NMR
chemical shift induced by incorporation of fluorine, the
significant 43Ca NMR signal change of Ca(II) ions and 1H
NMR signal change of OH- ions indicate that the fluorine
perturbs the chemical environment of Ca(II) ions and OH- ions
more than phosphorous atoms.
Poster 410
Synthesis and NMR Structural Characterization of a Novel
TEMPO Initiator for Surface Modification
Zhimin Yan
National Institute for Nanotechnology, Edmonton, Canada
Surface modification via polymer grafting with controlled
molecular weight and polydipsersity has attracted increasing
scientific interest. Among various surface modification
strategies, surface initiated polymerization is an excellent
method for the preparation of well-defined polymer structures.
Bearing this in mind, we designed a novel initiator structure
containing three general domains: a) surface anchoring
section (silane domain); b) TEMPO end group that propagates
with the growing of the chain; and c) nitroxide domain where
the monomer is inserted.
Poster 411
Contrast Enhanced Diffusion NMR – Determination of
Homopolymer Impurities in Block Copolymers
Rudy Wojtecki; Ankit Vora
IBM Almaden Research Center, San Jose, CA
The synthesis of block copolymers often suffer from
homopolymer impurities that can significantly affect
performance and are challenging to detect. Diffusion NMR
techniques (DOSY) can resolve different molecular weight
distributions of polymer mixtures. However, homopolymer
impurities can often be a similar molecular weight to the
respective block copolymer and overlapping proton signals
make determination of homopolymers challenging using
DOSY. We have taken advantage of the chemically distinct
units of block copolymers to facilitate micellization while
keeping homopolymer impurities soluble, resulting in two
distinct polymeric species that diffuse at significantly different
rates. This method allowed us to resolve the presence of
small amounts of homopolymer impurities in block copolymers
even with significant signal overlap.
Poster 412
Solid-state NMR Study of Organotellurium(IV)
Incorporation in Polyoxometalates
1
1
2
Banghao Chen ; Naresh Dalal ; Balamurugan Kandasamy ;
2, 3
2
2
4
Bassem Bassil ; Ali Haider ; Ulrich Kortz ; Jens Beckmann
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
1
2
Florida State University, Tallahassee, FL; Jacobs University,
3
Bremen, Geermany; University of Balamand, Tripoli,
4
Lebanon; Universität Bremen, Bremen, Germany
Organotellurium(IV) dihalides are well known and possess
many interesting properties such as easy handling, as well as
air, light and moisture stability, with rigid Te-C bonds and
easily hydrolysable Te-X bonds. Such features make them
interesting
functional
units
for
developing
novel
organotellurium-based organic-inorganic hybrid materials. The
first two organotellurium-containing polyoxometalates (POMs)
12[(C4H8Te (IV)) 3 (XIIIW 9O33) 2] (X = As, 1; Sb, 2) have been
prepared by simple and conventional procedures in good
yields.
The
cyclobutyltellurium(IV)-containing
heteropolyanions Polyanions 1 and 2 are isostructural with
three cyclobutyltellurium(IV) units being sandwiched between
two lonepair-containing POM fragments. As the compounds
are poorly soluble in common solvents, in this study they were
structurally characterized in the solid state by multinuclear
1
13
125
C,
Te) and other analysis
solid-state NMR ( H,
technologies.
Poster 413
Application of the CP along Z (ZCP)
27
31
Sequence to Al- P under MAS
1
2
2
Miwa Murakami ; Takayuki Kamihara ; Kiyonori Takegoshi ;
1
2
1
Hajime Arai ; Yoshiharu Uchimoto ; Zempachi Ogumi
1
2
Kyoto University, Uzi, Japan; Kyoto University, Kyoto, Japan
In this work, we demonstrate application of the recently
proposed CP sequence under MAS (CPZ: J. Magn. Reson.
27
31
245 (2014) 94) to Al- P. Since CPZ realizes magnetization
transfer among the Z magnetizations, it was expected that
CPZ is not significantly affected by the Z fluctuations, for
example, those aroused by the large anisotropic quadrupolar
interaction. We show that the original CPZ sequence is not
suitable for the present case and the modified CPZ sequence
utilizing the side-band matching condition, which we refer to
as the side-band CPZ sequence, is shown to be useful. It is
also shown that the effect of the quadrupolar interaction to the
apparent nutation frequency makes uniform enhancement
27
over different Al species difficult.
Poster 414
Solid-State NMR of Paramagnetic Materials above
100 kHz Magic Angle Spinning
1
3
2
Kevin Sanders ; Andrew J. Pell ; Bennett David ; Benno
2
2
2
2
Knott ; David Osen ; Alexander Krahn ; Armin Purea ;
2
2
3
Sebastian Wegner ; Frank Engelke ; Clare P. Grey ;
1, 4
1
Lyndon Emsley ; Guido Pintacuda
1
École Normale Supérieure de Lyon, Villeurbanne, France;
2
3
Bruker BioSpin, Rheinstetten, Germany; University of
4
Cambridge, Department of Chemistry, Cambridge, UK; École
Polytechnique Fédérale de Lausanne, Lausanne, Switzerland
We investigate here the advantages for the study of
paramagnetic materials offered by a new probe capable of
MAS rates higher than 100 kHz using a 0.7mm rotor.
Important benefits include (i) an improved averaging of dipolar
couplings and the separation of sidebands, with a spectacular
increase of both resolution, sensitivity and coherence lifetimes
compared to previously available MAS rates; (ii) the possibility
of reaching very large RF fields with very small amplifier
powers, with an astounding improvement in excitation
bandwidth and pulse efficiency; (iii) the completely new
possibility of applying broadband irradiation schemes which
are based on low-power RF elements. The approach is
demonstrated on a microcrystalline Tb(III) complex and a
Mn(II)-based paramagnetic battery cathode material.
Poster 415
Li MAS NMR of Composite Cathodes for Li-ion
Batteries:Effect of Enrichment on Low Concentration
Lithium Defect Sites Observation
Fulya Dogan; Brandon Long; Jason Croy; Kevin Gallagher;
Hakim Iddir; John Russell;
Mahalingam Balasubramanian; Baris Key
Argonne National Laboratory, Lemont, IL
Layered lithium- and manganese-rich, TM oxide intercalation
cathode structures have been widely investigated as the next
6
generation cathodes for advanced lithium-ion batteries. Li
NMR spectroscopy is the only structural probe currently
available that can quantitatively characterize local lithium
environments that dominates the free energy for site
occupation. In this study, we have undertaken an isotopic
enrichment strategy coupled with very long acquisition times
to obtain unprecedented, and quantitative, high-resolution
data for cycled electrodes using fully enriched cell
components. This strategy has allowed the determination of
structure-activity relationships and monitoring the evolution of
local order and low concentration defect formation that has a
profound effect on the overall electrochemical behavior.
6
Poster 416
+
Anion Effects on Li Solvation and Electrochemical
Behavior of Lithium-Sulfur Batteries
Kee Sung Han; Karl Mueller; Junzheng Chen; M.
Vijayakumar; Huilin Pan; Jie Xiao; Jun Liu
Pacific Northwest National Laboratory, Richland, WA
The effect of dissolved anions on lithium-sulfur (Li-S) battery
+
performance is related to the degree of Li -solvation when Li
salts with various anions are dissolved in DOL+DME
electrolyte solutions (1:1 by volume). Solvation effects were
17
studied by O NMR as well as by comparing the ratios of
NMR-determined diffusion coefficients of the ions and solvent
molecules. The data show the long-term performance of
+
lithium-sulfur batteries depends strongly on the degree of Li solvation of Li salt. While the initial performance of Li-S
batteries is mainly related to polysulfide (mainly Li2S8)
+
solvation. Our result suggests that the degree of Li -solvation
is more closely related to the Li-S battery performance than
the overall solubilities of either Li salts or Li2S8.
Poster 417
NMR Spectroscopy of "Challenging"
Group 15 Nuclei in Solids
1
2
Alexandra Faucher ; Victor V. Terskikh ;
1
Roderick E. Wasylishen
1
University of Alberta, Edmonton, Canada;
2
University of Ottawa, Ottawa, Canada
75
121/123
Several inorganic solids are investigated via As and
Sb
NMR spectroscopy, demonstrating the feasibility and
advantages of studying nuclei with large nuclear electric
quadrupole moments. Examples include the hexafluoride
salts KAsF6 and KSbF6, the structurally dissimilar Ph4AsBr
and Ph4SbBr, and a series of Lewis acid-base adducts.
11
Quadrupolar spin pairs in these adducts are studied via B
75
11
75
and As NMR spectroscopy, and B- As spin-spin coupling
interactions are quantified. In many of these examples,
75
central transition (mI = 1/2 to mI = −1/2) linewidths in As and
Page 117
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
121/123
Sb NMR spectra are on the order of MHz at B0 = 21.14
75
T. CQ values determined in this work range from CQ ( As) = 0
Hz, in cubic KAsF6, to ca. 194 MHz in Ph3As.
Poster 418
A Wide Line, Static, Solid State NMR Study of α-NaY1xYbxEryF4
Timothy Newman; Michele Martin; Ming Zhang; Gang-yu Liu;
Matthew Augustine
University of California, Davis, Davis, CA
19
Ultra-wide line, static, F solid state NMR spectroscopy is
used to probe local chemical structure in rare earth doped αNaY1-xYbxEryF4. It is the L ≠ 0 rare earth dopants that both
19
broaden and shift the F NMR spectrum. In some cases the
19
F hole burning
spectrum spans over 10,000 ppm.
experiments suggest that the NMR response in these systems
is inhomogeneously broadened and that the “on-resonance”
portion of the spectrum does not experience a contact shift,
facts that are used to relate the rare earth content dependent
T1 value to simple paramagnetic ion occupation statistics in a
model 6 nm diameter α-NaY1-xYbxEryF4 nanoparticle.
Poster 419
NMR Fingerprinting of Zeolite Framework Topology by
One and Two-Dimensional Solid-State
Francis Taulelle
Univ. Versailles, Versailles Cedex, France
The potential of 1D 29Si and 2D 29Si-29Si and 29Si-17O
NMR as graph-invariants for fingerprinting zeolite frameworks
has been explored. 1D and 2D 29Si NMR provide graph
vertices, edges and the adjacency matrix. Hypothetical 1D
29Si and 2D 29Si-29Si NMR signatures for 193 zeolite
frameworks have been generated. It shows that with 1D 29Si
NMR data only, almost 20% of zeolite frameworks could be
distinguished. Further NMR signatures were generated with
2D 29Si-29Si and 29Si-17O correlations allowing up to 80%
of the listed zeolites could be unambiguously discriminated.
Conclusions: (i) solid-state NMR data represent strong graph
invariants for zeolite framework, (ii) 29Si and 17O NMR
measurements are worth being investigated for zeolites
structure resolution.
Poster 420
1
13
High Resolution H and C Probing of the Mechanism of
Ferroelectric Phase Transition in MOFs with the
Perovskite Architecture
2
1
1
Nandita Abhyankar ; Jin Jung Kweon ; Eun-Sang Choi ;
1
1, 2
Riqiang Fu ; Naresh Dalal
1
National High Magnetic Field Laboratory, Tallahassee, FL;
2
Florida State University, Tallahassee, FL
Metal-Organic Framework (MOF) compounds, have become a
focus of increasing research interest, for H2 storage, and
unusual sources of memory storage and manipulation, using
both electric and magnetic controls. One such family is based
on the inorganic perovskite system, ABO3, a model is
[CH3NH2]Zn (HCO2) 3 ( ZnMOF). Dielectric and heat capacity
studies showed that ZnMOF is ferroelectric and glassy,
closely resembling the inorganic analogues. To examine the
13
C NMR
details we carried out VT high resolution
measurements on ZnMOF, and observed spectacular
dynamic effects on approaching its ferroelectric transition
around 156 K. Line shape analysis using modified Bloch
equations yields τc and EA , and direct clues to the
mechanism.
Page 118
Poster 421
Integration Standard for MAS-NMR Investigations
Lingyu Chi; Robert Block; Sierra Herndon; Rex Gerald; Klaus
Woelk
Missouri University of Science and Technology, Rolla, MO
The amount of boron in an anhydrous B2O3-DMF solution was
determined from MAS-NMR experiments employing MASCapPacks. In a control experiment we inserted an empty
borosilicate glass capillary tube (integration standard) into a
MAS rotor and using signal subtraction obtained a sharp
11
integration peak. In the B MAS qNMR experiment of a B2O3DMF solution, we inserted a borosilicate glass capillary tube
filled with a solution of B2O3 in DMF into a B2O3-filled MAS
rotor, and determined the boron content of the B2O3 solution
in the presence of static (boron nitride stator) and dynamic
(solid B2O3 in the rotor) boron NMR background signals.
INSTRUMENTATION
422 - 469
Poster 422
Multiple On-line NMR System Development for Direct
Alcohol Fuel Cells
1, 2
1, 2
Ryeo Yun Hwang ; Oc Hee Han
1
2
Korea Basic Science Institute, Seoul, South Korea; GRAST,
Chungnam National University, Daejeon, Korea
The results of the in situ/on line investigation of fuel cell
exhausts often have limitations with a focus on a single side of
the system, therefore, not providing simultaneous detection of
chemicals in the fuel cell exhausts of both electrodes. This
work reports the simultaneous chemical detection for anode
and cathode exhausts using the on-line NMR system
developed for NMR detection of multiple samples at the same
time. We used two dimensional 2H-NMR spectroscopy to
simultaneously observe chemicals present in the liquid anode
and cathode exhausts of DMFCs. Our results demonstrate
application of this on-line NMR system can be extended to
other chemical systems with multiple chemical flows such as
the flow batteries and the combinatorial chemistry.
Poster 423
Overhauser Dynamic Nuclear Polarization (ODNP)
Enhanced NMR at 0.35 T
Thomas Casey
University of Florida, Gainesville, FL
Following the lead of the Han group at the University of
California Santa Barbara, we assembled a custom high power
X-band (9.85 GHz) MW transmitter for performing ODNP
enhanced 1H NMR experiments at 14.9 MHz. Our
experimental setup includes a Bruker E500 X-band EPR
spectrometer, a tecmag Apollo HF-2 NMR console with
custom probes that are interfaced with EPR resonators, and a
custom high power X-band MW source (~ 5 Watts). Work from
the Han group (among others) has led to refined methods for
application of this technique and a corresponding theoretical
framework for analyzing the data. Here we present our latest
developments and applications of these methods. In
particular, an EPR resonator/NMR probe design for alleviating
current experimental challenges.
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
Poster 424
ATL Medium Pressure Helium Recovery System for NMR
Labs
Shi Li; Grant Rayner; Jeremy Terry; Cesar Chialvo; Jost
Diederichs; Martin Kugler; Stefano Spagna
Quantum Design, San Diego, CA
For helium recycle in NMR labs with smaller magnets,
Medium Pressure Recovery (MPR) system offers advantages
such as small footprint, low pressure (80 psi), and being a
fully contained system. It is designed to capture both static
boiloff and refill transfer boiloff with greater than 90%
efficiency. As demonstrated by the installation in an NMR Lab
at UC Davis, the MPR system is compact enough to be
treated as a laboratory equipment, thus easy to install and
manage. It automatically handles the transitions between
static state with low boiloff, and transfer state with high boiloff,
by adjusting its booster speed according to the helium flow
rate. The modular subcomponents of the MPR can be
expanded to accommodate multiple NMR systems.
Poster 425
An Optical Multi-channel Receiver for Magnetic
Resonance Imaging by Wavelength Division Multiplexing
Zhu Xiaoyun; Wang Weimin
Institute of Quantum Electronics Peking University,
Beijing, China
A
new
method
based
on
wavelength
division
multiplexing(WDM) technology is proposed to receive and
transfer multi-channel signal of parallel magnetic resonance
imaging(MRI). Compared with the foregoing time division
multiplexing(TDM) and frequency division multiplexing(FDM)
methods using conventional coaxial cable, the proposed
method has advantages of simpler structure, compact size,
fast speed and cost effectiveness. In addition, the transmitter
module has been integrated inside the MRI receiving coil
which decreases the cable loss to the minimum. As an
implement example, a 4-channel receiver with optical WDM
technology has been built and tested in MRI system. The SNR
of optical WDM method is improved by 15% approximately
with a distinct imaging quality. The proposed method is easy
to expend to more channels.
Poster 426
Design and Simulation of a
Multilayer Halbach Magnet for NMR
Qiaoyan Chen
SIBET, CAS, Suzhou, China
In this paper, firstly the model for odd layers Halbach cylinders
is proposed. Then an approach of searching for the optimum
interlayer distances of multilayer Halbach cylinders is
presented, of which the main procedure includes: genetic
algorithm calculation, optimization in software Mathcad and
finally, verification by an example in software Maxwell.
Moreover, the disturbance of uniformity in 5 mm DSV
(Diameter of Spherical Volume) is presented with errors. As a
result, the minimum uniformity of 5 mm DSV is achieved 66
ppm ideally, and it is about 128 ppm practically in simulating
the actual engineering model with errors in symmetric
distribution. This Halbach magnet with odd layers has a good
performance, and may find potential applications in NMR.
Poster 427
A New ASTM Standard Practice For Liquid State NMR
Instruments
1
2
3
4
Dan Bearden ; George Gray ; Roy Hoffman ; Gary Kramer ;
5
Patrick Tishmack
1
2
NIST, Charleston, SC; NMR Consultant, San Francisco Bay
3
Area, CA; The Hebrew University of Jerusalem, Jerusalem,
4
5
Israel; REMARKramer, Inc, Gaithersburg, MD; SSCI, West
Lafayette, IN
A new ASTM Standard Practice for Measuring and Reporting
Performance of Fourier-Transform Nuclear Magnetic
Resonance (FT-NMR) Spectrometers for Liquid Samples
E2977-14 has been released. This new standard practice
contains requirements for liquid NMR test samples, for their
certificates of analysis, and for their use in determining and
reporting the performance of FT-NMR spectrometers
operating over the range of 200 MHz to 1200 MHz.
Poster 428
1
19
Achievement of H- F Heteronuclear Experiments using
the Conventional Spectrometer with a Shared Single High
Band Amplifier
1
2
3
Mitsuru Tashiro ; Chiseko Sakuma ; Jun-ichi Kurita ;
4
Kazuo Furihata
1
2
Meisei University, Hino, Japan; Tokyo University of
3
Pharmacy and Life Sciences, Hachioji, Japan; Agilent
4
Technologies Japan, Ltd., Tokyo, Japan; University of Tokyo,
Tokyo, Japan
1
19
The H- F heteronuclear NMR experiments were achieved
using the conventional spectrometer equipped with a single
high band amplifier and a H/F/C-double tuned probe.
Although double high band amplifiers are generally required to
perform such experiments, a simple modification of pathway
in the conventional spectrometer was capable of acquiring
1
19
various H- F heteronuclear spectra. The efficiency of the
present technique was demonstrated in an application for
19 1
1
19
F{ H} and H{ F} saturation transfer difference experiments.
Poster 429
A Single Channel Spiral Volume Coil for in vivo Imaging
of the Whole Human Brain at 6.5 mT
1, 2
1, 2
Cristen LaPierre ; Mathieu Sarracanie ; David
1, 3
1, 2
Waddington ; Matthew Rosen
1
MGH/A.A. Martinos Center for Biomedical Imaging,
2
Charlestown, MA; Department of Physics, Harvard
3
University, Cambridge, MA; School of Physics, University of
Sydney, Sydney, Australia
MRI at low magnetic field (<10 mT) without cryogenic or
hyperpolarization techniques presents unique engineering
challenges. Imaging coils must maximize coverage over the
volume of interest while minimizing losses in a regime unusual
in contemporary MRI—where Johnson noise dominates the
noise floor. We present a new design for a spiral volume coil
design for combined Tx and Rx and optimized for human
head imaging in the transverse 6.5 mT B0 field of our low field
scanner. A 30-turn single channel volume litz-wire spiral coil
designed for low field imaging significantly outperformed our
8-channel array coil. By minimizing losses in the coil,
maximizing filling factor and eliminating coupling issues, we
were able to obtain significantly higher SNR.
Poster 430
High Performance Probe for in vivo Overhauser MRI
1, 2
1, 3
1,
David Waddington ; Mathieu Sarracanie ; Najat Salameh
3
1, 3
; Matthew Rosen
1
MGH/A.A. Martinos Center for Biomedical Imaging,
2
Charlestown, MA; School of Physics, University of Sydney,
Page 119
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
3
Sydney, Australia; Department of Physics, Harvard
University, Cambridge, MA
Overhauser-enhanced MRI (OMRI) is an electron-proton
double resonance imaging technique of much interest due to
its ability to detect the concentration and distribution of free
radicals. Tracking of exogenous free radicals with OMRI in
vivo has enabled the development of oxymetry probes and the
imaging of redox reactions. The large gyromagnetic ratio of
electrons (28 GHz/T) demands that in vivo OMRI is performed
at very low magnetic fields (~10 mT) in order to minimize RF
heating and penetration depth issues. We report here
development of a high performance OMRI probe consisting of
a litz wire NMR solenoid (276 kHz) inside a modified
Alderman-Grant Resonator (141 MHz) for operation at 6.5
mT.
Poster 431
Sensing Thermal Conductivity with Nanoscale Resolution
via a Scanning Spin Probe
1
1
2
Abdelghani Laraoui ; Halley Aycock-Rizzo ; Xi Lu ; Elisa
2
1
Riedo ; Carlos Meriles
1
2
CUNY, New York, NY; Georgia Institute of Technology,
Atlanta, GA
New forms of nanoscale magnetic resonance imaging are
being developed that exploit the properties of select
paramagnetic centers within crystal hosts. Here we use a
diamond-nanoparticle-hosted NV center as a local
temperature sensor at the apex of a silicon thermal tip. We
apply an electrical current to heat up the tip and rely on the
NV to monitor the small thermal changes the tip experiences
as it is brought into contact with surfaces of varying thermal
conductivity. With the aid of an AFM/confocal setup, we image
phantom microstructures with nanoscale resolution, and attain
excellent agreement between the thermal conductivity and
topographic maps. We anticipate multiple applications
including, e.g., the investigation of phase transitions and
chemical reactions in various solid-state systems.
Poster 432
400 MHz (9.4 T) Cryogen Free Magnet for High Resolution
Solid State NMR
1
1, 2
1
Eugeny Kryukov ; James McDonald ; Stephen Burgess ;
1
2
1
David Phillipps ; John Hanna ; Jeremy Good
1
2
Cryogenic Ltd, London, UK, London, UK; University of
Warwick, Coventry, UK
Cryogen free magnet for 9.4 T was designed and
manufactured by Cryogenic Ltd. The magnet was wound with
standard NbTi wire and suspended inside a dry cryostat in
vacuum. This design allowed making the cryostat much more
compact with total weight a small fraction of conventional
liquid ones. The Pulse Tube cold head driven by a
compressor keeps the magnet cold in superconductive state.
Permanently installed current leads make the magnet ready
for field sweep experiments. Cryogen free technology
eliminates the need of liquid helium supply. The magnet is
actively shielded by compensation coils incorporated into
main current circuit. Short height allows customers to load
their standard MAS from the top as well as from the bottom of
the cryostat.
Poster 433
A Microcoil-based NMR Probe Head for Automated and
Reproducible in-field PHIP/SABRE Experiments
Page 120
1
3
Lorenzo Bordonali ; Philipp Rovedo ;
3
1, 2
Jan-Bernd Hoevener ; Jan Korvink
1
Freiburg University, IMTEK, Freiburg Im Breisgau, Germany;
2
Freiburg Institute of Advanced Studies (FRIAS), Freiburg im
3
Breisgau, Deutschland; Medical Physics, Uniklinik-Freiburg,
Freiburg, Germany
We present a custom NMR probe head for SABRE/PHIP
experiments where the pH2 polarizer is closely positioned to a
micro NMR detector and fluidically connected to it, allowing for
very short sample shuttling times (less than 1s). The polarizer
is a bubbling and storage chamber, where pH2 gas is bubbled
in through a thin capillary. A waste chamber located at the
other end of the fluidic line collects the used solution. Control
over the measurement rig, including fluids and gases
manipulation, is handled directly from a Bruker spectrometer
pulse sequence automation program, allowing for very precise
timing of automated events and assuring a high degree of
reproducibility of the hyperpolarization experiment.
Poster 434
Ultra-Low-Field NMR Detection Using MagnetoImpedance Sensors
Reza Tavakoli Dinani; Mike Hayden
Department of Physics, Simon Fraser University,
Burnaby, BC, Canada
We have used magneto-impedance (MI) sensors for detection
of nuclear magnetic resonance (NMR) phenomena. Our
1
experiments are performed on the H nuclei in a continuous
flow of water that is pre-polarized in a 1.5 T magnetic field and
then guided to a well-shielded low-field volume in which the
MI sensors reside. Up to one-quarter of the nuclear
magnetization leaving the polarizer reaches the sensors. En
route, adiabatic fast passage techniques are used to
periodically invert the magnetization, at rates up to 30 Hz.
NMR tipping pulses are also applied at Larmor frequencies
below 1 kHz. The resulting variations in magnetic field
associated with the longitudinal component of the nuclear
magnetization are readily resolved by the MI sensors.
Poster 435
An X0 Shim Coil for Precise Setting of the Magic Angle
1
2
1
Tatsuya Matsunaga ; Takashi Mizuno ; K. Takegoshi
1
2
Kyoto University, Kyoto-Shi, Japan; JEOL Resonance Inc.,
Akishima, Tokyo, Japan
In high-resolution solid-state NMR, magic angle spinning
(MAS) is an indispensable technique to remove anisotropic
interaction and requires fine adjustment of the spinning angle.
We introduce a new method for precise setting of the magic
angle by using a saddle coil. The coil, which is referred to as
an X0 shim coil, is wound to produce a uniform static
magnetic-field Bx perpendicular to the main magnetic field B0.
The magnetic field felt by a sample is a vector sum Bx and B0,
and the spinning angle can be precisely adjusted by current
supplied to the X0 shim coil. It is shown that the resolution of
o
the adjustable angle achieved by our X0 shim coil is 0.0093
per 1 A.
Poster 436
Multi-chromatic Magnetic Resonance Imaging Using
Frequency Lock-in Suppression
Yu-Wen Chen; Dennis Hwang
Dpet. of Chem. & Biochem, National Chung Cheng Uni, ChiaYi, Taiwan
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
An electronic feedback device that generates a specific
narrow frequency bandwidth RF field is presented.
Spectroscopy and imaging experiments were performed.
Frequency tuning allowed the selected spectral peak to be
suppressed. Phantom tests using methanol, ethanol, and
water showed different contrasts using different feedback RF
field frequencies. The contrast achieved in in vivo mouse
brain imaging indicated a better spatial discrimination when
compared with the conventional imaging methods, especially
in the hippocampus region. Selective lock-in suppressed
imaging provides frequency information rather than
determining an object’s evolution over time and allows small
susceptibility variations to be distinguished by tuning the
frequency of the narrow bandwidth lock-in RF field.
Poster 437
A Disposable Fluidic Insert with Integrated Microwave
Resonator for Ku-band Applications
1, 2
1, 2
1, 2
Sebastian Z. Kiss ; Markus V. Meissner ; Nils Spengler ;
1, 2
Jan G. Korvink
1
2
University of Freiburg - IMTEK, Freiburg, Germany; Institute
for Microstructure Technology - IMT, Karlsruhe, Germany
In this work we present a first prototype of a double split-ring
type resonator for Ku-band applications. The microwave (MW)
resonator is directly integrated onto a compact fluidic insert.
The fabrication process is simple and cost efficient rendering
the chip suitable for single use applications. We report on
typical quality factors as well as possible frequency tuning
mechanisms for the proposed MW resonator type.
Poster 438
Single Step Mold and Metal Patterning for ElectroDeposition Enables Rapid and Low-Cost
Fabrication of MR Field Coils
Markus Meissner; Nils Spengler; Dario Mager; Sebastian
Kiss; Peter While; Jan Korvink
University of Freiburg, Freiburg, Germany
We introduce a new micro-structuring process, particularly
suitable for the rapid fabrication of planar NMR antennas,
shim coils and gradient coils. Our process is based on a
droplet based deposition technique of conductive silver nano
particle ink. Structuring of electrically conductive tracks is
performed instantly, by printing silver ink on cured photodefinable film resist. Molds for electroplating are patterned into
thick-film photo-definable resist via backside exposure and
our printed structures serve as both the shadow mask for the
mould, and the seed layer for the electroplating. As a
demonstration of our low-cost and precise micro fabrication
process, a planar micro-coil for 1H spin excitation and
reception was fabricated.
Poster 439
A Multiple-Tuned Micro Helmholtz Detector for MRI and
2D NMR of 100nl Liquid Samples
1
1
2
1
Jens Höfflin ; Nils Spengler ; Vlad Badilita ; Neil MacKinnon ;
1
Jan Korvink
1
Laboratory for Simulation - University of Freiburg, Freiburg,
2
Germany; Laboratory for Microactuators
University of Fr, Freiburg, Germany
How can Helmholtz microcoils be flexibly extended for X­nulei NMR and MRI? To show this, a double tuned coil was
developed based on the Helmholtz device of Spengler et.al.
The coil was made multi resonant by adapting circuits from
Kan et.al. to a 500 MHz Bruker widebore NMR. The coil was
integrated onto an insert that fits inside the Bruker Micro 5
probehead gradient, so that NMR as well as imaging
experiments could be performed for liquid samples of 100nl.
Poster 440
An MR-Compatible Microscope for Simultaneous DualMode Optical and MR Microscopy
1
2
1
Matthias C Wapler ; Frederik Testud ; Nils Spengler ; Maxim
2
1
Zaitsev ; Ulrike Wallrabe
1
University of Freiburg, IMTEK, Freiburg, Germany;
2
University Medical Centre Freiburg, Freiburg, Germany
We present an optical microscope with an integrated MR
probe that is designed to operate inside a small animal MR
scanner without interfering with simultaneous MR
measurements. Using an adaptive lens, the microscope can
focus through the depth of the sample. Depending on the
configuration, the optical field of view is 0.6mm³ to 2mm³ at a
resolution of 0.6 to 2µm, with apochromatic color correction
and no geometric distortion. The magnetic field distortion is
19ppb (RMS) over the sample region. Different MR probes
can be integrated with little modification, or conventional
volume RF coils can also be used. We demonstrate the
simultaneous imaging of 10µm to 50µm beads; potential
applications include small in-vivo organisms like C. Elegans or
zebrafish embryos.
Poster 441
Near Earth-Field NMR via Multi-Pass RF Atomic
Magnetometer
Merideth Frey; Nezih Dural; Michael Romalis
Princeton University, Princeton, NJ
Near Earth-field NMR spectroscopy remains a challenging
and enticing regime. At these field strengths, both internal and
external spin interactions significantly affect the spectrum,
maximizing the amount of encoded information, but also
requiring new detection techniques. Atomic magnetometers
offer the best magnetic sensitivity at low fields, but one must
account for the different gyromagnetic ratios of the atomic and
nuclear spins. We discuss a new method for off-resonant
NMR detection with a multi-pass RF atomic magnetometer
with minimum sensitivity loss. This method can potentially be
used to resolve chemical shifts for magnetic fields near
Earth’s field and is a great step towards an inexpensive NMR
system with the potential to provide the combined chemical
information of high and low-field regimes.
Poster 442
Double-Resonance HTS Coils toward Dual-Optimized
High-Sensitivity NMR Probes
1, 2
2
3,
Vijaykumar Ramaswamy ; Jerris Hooker ; Richard Withers
4
3, 5
2
1, 2
; Robert E. Nast ; William W. Brey ; Arthur Edison
1
2
University of Florida, Gainesville, FL; National High
3
Magnetic Field Laboratory, FSU, Tallahassee, FL; Past
4
Affiliation: Agilent Technologies, Santa Clara, CA; Current
5
Affiliation: Maxim Integrated, San Jose, CA; Current
Affiliation: Out of the Fog Research, Mountain View, CA
NMR probes based on high-temperature superconductors
(HTS) provide significant gains in sensitivity. HTS coils are
patterned out of thin-film YBCO on planar sapphire
substrates. We recently reported a HTS-based 1.5-mm probe
13
optimized for C detection. This probe achieves highest
13
mass-sensitivity for C, while sensitivity of other channels is
compromised due to the orthogonal nesting of coils around
the sample. Novel double-resonance coils are required in
Page 121
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
order to optimize the sensitivity of two channels. We are
currently developing a 1.5-mm probe simultaneously
1
13
optimized for both H and C sensitivity using doubleresonance coils. Coil design considerations as well as probe
performance will be presented in this work.
Poster 443
Two-Center NMR Magnet by Integration of Ferromagnetic
Shimming Inserts
1
2
1
Herbert Ryan ; Jan Van Bentum ; Thorsten Maly
1
2
Bridge12 Technologies, Inc., Framingham, MA; Radboud
University, Nijmegen
This work presents the design and realization of a novel twocenter high-field NMR magnet, for use in Dynamic Nuclear
Polarization (DNP) NMR experiments. A 9.4 Tesla wide bore
magnet is outfitted with ferromagnetic steel shimming inserts
which reach flux saturation to create a lower field strength at
the position of the NMR sample, thus creating an inexpensive
two-center magnet (where the lateral isocenter is occupied by
the microwave radiation source).
Poster 444
Helium Recovery in an NMR Lab
David Live; John Glushka; James H. Prestegard
University of Georgia, Athens, GA
Several recent disruptions in helium supplies, along with its
increasing cost, and value as a non-renewable resource, have
led NMR labs to consider helium recovery. A desirable
solution for an NMR lab with multiple existing instruments and
no access to institution-wide recovery is a recovery system of
appropriate capacity and physical size for a single lab. A little
over a year ago we installed a system designed to collect the
ambient helium gas evolved from six NMR magnet cryostats
as well as the boil-off generated during fills. The purifier and
the liquefier use the same type of coldhead commonly found
in cryoprobes, presenting similar maintenance requirements.
Our experience with recovery and maintenance over the past
year will be reported.
Poster 445
1
13 2
15
Quadruple-Resonance ( H/ C/ H/ N) 800MHz MAS NMR
Probe
1
1, 2
1
Kelsey Collier ; Catalina Espinosa ; Rachel W. Martin
1
2
University of California at Irvine, Irvine, CA; Yale University,
New Haven, CT
1
13 2
15
A quadruple-resonance ( H/ C/ H/ N) magic-angle spinning
solid-state NMR probe has been developed. The probe
13
15
2
incorporates two coaxial coils. The C, N, and H channels
are balanced across a solenoid coil to maximize signal
13
2
15
strength, giving C/ H/ N high power-handling capabilities.
1
The H channel utilizes a modified Alderman-Grant coil to
minimize the inductive heating of biological samples. The
probe design utilizes transmission line segments as tuneable
reactances. Partial deuteration of samples is commonly used
1
1
to reduce H- H dipolar couplings; this probe will be capable
of direct detection on deuterium. Multidimensional
experiments can be used to obtain site-specific order
2
2
parameters from the H quadrupole moment. The rapid H
relaxation time will allow a faster magnetization transfer time
in correlation experiments.
Poster 446
A Millimeter-wave Tunable Cavity for Ultra-sensitive DNPNMR at Low Budget
Page 122
1
1
2
Paul Ellis ; George Entzminger ; Alexander A. Nevzorov ;
2
1
1
1
Alex I. Smirnov ; John Staab ; Laura Holte ; F. David Doty
1
2
Doty Scientific, Inc., Columbia, SC; North Carolina State
University, Raleigh, NC
Our detailed simulations of a novel millimeter wave (mmw)
DNP cavity have shown the potential for achieving the needed
electron spin saturation with two orders of magnitude lower
microwave power than the existing MAS-DNP designs, with a
novel DNP cavity that is initially compatible only with static
(non-spinning) methods.
The static DNP cavity and probe being developed (7
T), is expected to yield two orders of magnitude gain in S/N,
for a total entry budget of under $180K, including the 0.05-0.3
W solid-state mmw source, DNP probe, waveguides, and
transitions.
The presentation will focus on a rigorous approach to
DNP cavity optimization using full-wave simulation tools for
maximizing S/N. Results from bench experiments provide
preliminary validations of the simulation methods.
Poster 447
Sensitivity Enhancement of an Inductively Coupled Local
Detection Coil using a Negative Resistance Amplifier
1
2
1
Joseph Murphy-Boesch ; Chunqi Qian ; Qi Duan ;
1
Stephen Dodd
1
2
NIH, NINDS, LFMI, Bethesda, MD; Department of
Radiology, Michigan State University, East Lansing, MI
A single-port, negative resistance amplifier has been
constructed and connected to an isolated detection coil tuned
for 3T. Positive feedback from a GaAs transistor transforms
capacitance on its source to negative resistance on its gate,
providing current amplification in the coil. In the case of strong
coupling to an external receive loop, the signal is enhanced,
providing an SNR comparable to a directly connected coil. A
prototype coil for imaging of a mouse brain provided 14 dB of
current gain while consuming only 90 uW of power. Highresolution MR images of the mouse brain were acquired using
a clinical surface array to receive signals, providing an order
of magnitude increase in local SNR as compared with the
clinical array alone.
Poster 448
A New High-Throughput Multiple Sample NMR Probe
Design for Solids
1, 2
1
Matthew Nethercott ; Eric Munson
1
2
University of Kentucky, Lexington, KY; Revolution NMR, Fort
Collins, CO
In CPMAS NMR spectroscopy, the time used for data
acquisition is typically an order of magnitude less than the
time needed for the nuclei to relax back to equilibrium. In
order to better utilize this time, we have developed a fully
shielded, non-moving high-throughput solids probe that can
accommodate between 2-5 spinning modules. The unique
feature of this probe is that the RF of each of the individual
probe circuits is entirely self contained, which is achieved by
placing the spinning modules in copper tubes. The copper
shielding around the modules prevents RF crosstalk, and not
moving the probe prevents the generation of large eddy
currents. This probe design is applicable to all SSNMR work
at any magnetic field strength.
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
Poster 449
1H-31P Birdcage Volume Coil with Adjustable Sliding
Ring Tuner for in vivo imAging and
Spectroscopy at 17.6 T
1
3
4
Malathy Elumalai ; Guita Banan ; Aditya Kasinadhuni ; Kulam
5
6
6
1, 2
Magdoom ; Peter Gor'Kov ; William Brey ; Thomas Mareci
1
2
McKnight Brain Institue, Gainesville, FL; Department of
Biochemistry and Molecular biology, Gainesville, FL;
3
4
Department of Physics, Gainesville, FL; Department of bio5
medical Engineering, Gainesville, FL; Department of
6
Mechanical and Aerospace Engg, Gainesville, FL; National
High Magnetic Field Laboratory, Tallahassee, FL
For a 17.6 T vertical magnet, a transmit-receive, singlebirdcage volume resonator was constructed for 1H-31P
imaging and spectroscopy in vivo. For the 1H channel (750
MHz), a large tuning range was obtained with a sliding ring
design of distributed capacitance (Qian). For the 31P channel
(303 MHz), a low-pass birdcage was constructed, using chip
capacitors, and inductively coupled to the transmitter-receiver.
The resonator, part of a modular probe, can be tuned and
matched in the magnet. With the wider tuning range and field
homogeneity of this resonator design, the measurement of
images and spectra in vivo with 1H and low gamma nuclei
(such as 31P) become feasible at high field strength.
Poster 450
Portable MRI Scanner using Rotating Spatial Encoding
Magnetic Fields: Extension to 3D Imaging using Transmit
Array Spatial Encoding (TRASE)
1, 3
1, 2
Clarissa Zimmerman Cooley ; Jason Stockmann ; Mathieu
1, 2
1, 2
1, 3
Sarracanie ; Matthew Rosen ; Lawrence Wald
1
MGH / A. A. Martinos Center for Biomedical Imaging,
2
Charlestown, MA; Dept. of Physics, Harvard University,
3
Cambridge, MA; Harvard Medical School, Boston, MA
A low-cost portable MRI scanner for brain imaging could
facilitate imaging in sites that are unsuitable for traditional
scanners. Transmit array spatial encoding (TRASE) has been
incorporated into a previously presented scanner which uses
a rotating, lightweight, inhomogeneous magnet to do 2D
generalized projection imaging. The combination of TRASE
and the rotating Spatial Encoding Magnetic field (rSEM)
method is used to produce proof-of-concepts 3D images. In
future work, the magnet will be slightly enlarged to
comfortable fit a human head and the necessary RF coils. The
low-cost, portable scanner architecture is enabled by allowing
the magnet to be low-field and inhomogeneous, and by
eliminating the need for gradient coils and gradient power
amplifiers through the rSEM and TRASE methods.
Poster 451
Chemical Shift Imaging with Sub-Nanoliter Voxels:
Spectral versus Spatial SNR
Nils Spengler; Ulrike Wallrabe; Jan Korvink
IMTEK, University of Freiburg, Freiburg I Br, Germany
We present chemical shift imaging of two different liquids
using a custom-made micro probe setup consisting of a
1.2mm diameter micro Helmholtz coil-pair and an
exchangeable microfluidic sample container with an active
volume of 110nL in combination with a commercially available
micro-imaging system. In total, two experiments were
performed, the former with 1.44nL voxel volumes and the
latter with 0.36nL voxels. For both experiments, spectral
peaks were successfully assigned in the expected region and
represented by a colour map. The increased spatial resolution
of the second experiment is, however, paid by an increase of
acquisition time and a decrease of SNR and hence is a tradeoff between these parameters, ultimately narrowing down
possible fields of application at increasing spatial resolution.
Poster 452
Progress towards 1.5 GHz NMR user Facility at the
National High Magnetic Field Laboratory
Ilya Litvak; Peter L. Gor'kov; Zhehong Gan; Timothy A. Cross;
William W. Brey; Mark D. Bird
National High Magnetic Field Lab / FSU, Tallahassee, FL
A new powered resistive-superconductive hybrid magnet is
scheduled to reach 36 T (1.5 GHz proton frequency) in 2016.
The magnet will achieve 1 ppm homogeneity across the
sample and will feature an active field regulation system.
Ultra-high magnetic field will cause a dramatic increase in
spectral resolution and sensitivity of half-integer quadrupolar
isotopes, benefit proton-detected spectroscopy of proteins
and spectroscopy of unreceptive nuclei.
Probes are being developed for the new magnet for biological
and materials applications. We report on progress towards
NMR at 1.5 GHz. We welcome proposals for experiments at
ultrahigh field. Scientists can apply for free-of-charge access
to
magnet
time
on
our
spectrometers
at
https://users.magnet.fsu.edu/.
Poster 453
Movable Hyperpolarized Xenon System for Human
NMR/MRI @ WIPM
Xianping Sun; Xiuchao Zhao; Huiting Zhang; Yaping Yuan;
Junshuai Xie; Xian Chen; Zhao Li; Chaohui Ye; Xin Zhou
Wuhan Inst. of Physics and Mathematics, CAS,
Wuhan, Hubei, China
Spin-exchange optical pumping technique is able to enhance
the nuclear spin polarization by four or five orders of
magnitude, which tremendously improves the sensitivity of
NMR/MRI. Building a high-performance hyperpolarizedxenon
system and gas delivery system is vital for the high-sensitive
human lung NMR/MRI. WIPM (Wuhan Institute of Physics and
Mathematics) developed a novel mobile hyperpolarized xenon
system for human NMR/MRI research, which includes
homebuilt one-dimensional fourth-ring coils, gas ventilation
and delivery system, two-body alkali-xenon cell and gas
storage system. The NMR signal of hyperpolarized xenon gas
is enhanced more than 40,000 in comparison to the thermal
one. We got lung images of human with our hyperpolarized
xenon system.
Poster 454
1020 MHz LTS/HTS NMR: II. Application to
Solid-State NMR
1, 2
2
3
Yusuke Nishiyama ; Manoj Kumar Pandey ; Pierre Florian ;
3
4
4
4
Franck Fyon ; Kenjiro Hashi ; Shinobu Ohki ; Gen Nishijima ;
4
4
4
Shinji Matsumoto ; Takeshi Noguchi ; Kenzo Deguchi ;
4
4
5
Atsushi Goto ; Tadashi Shimizu ; Hideaki Maeda ; Masato
5
5
1
Takahashi ; Yoshinori Yanagisawa ; Ryoji Tanaka ; Takahiro
1
1
1
Nemoto ; Tetsuo Miyamoto ; Hiroto Suematsu ; Kazuyoshi
6
6
Saito ; Takashi Miki
1
2
JEOL Resonance Inc., Tokyo, Japan; RIKEN CLST-JEOL
Collaboration Center, Yokohama, Kanagawa, Japan;
3
4
CEMHTI-CNRS, Orleans Cedex 2, France; National Institute
Page 123
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
5
for Materials Sciences, Tsukuba Ibaraki, Japan; RIKEN
6
CLST, Yokohama, Japan; Kobe Steel Ltd., Kobe, Japan
We successfully break the barrier of 1.0 GHz by using hightemperature superconductor (HTS) magnet. HTS enables us
1) very high magnetic field at more than 1.0 GHz, 2) stable
and homogeneous field, 3) long time operation, and 4) low
energy consumption. Half-integer quadrupolar nuclei enjoy the
high magnetic field where the second order quadrupolar
broadening is greatly suppressed. Combination of ultra-high
magnetic field and ultra-fast MAS (>100 kHz) is another very
exciting research area. In both cases, the long term operation
enables us to run long-term multi-dimensional measurements,
which is impossible at previous resistant magnet for more
than 1.0 GHz.
Poster 455
High-Field NMR Experiments Performed on a
Zero-Ultralow Field NMR Spectrometer
1, 2
3
2
Michael Tayler ; Tobias Sjolander ; Lynn Gladden ; Alex
4
5, 6
Pines ; Dmitry Budker
1
2
UCB Physics, Berkeley, CA; MRRC University of
3
Cambridge, Cambridge, UK; UCB Chemistry, Berkeley, CA;
4
5
UCB Chemistry, MSD LBNL, Berkeley, CA; Helmholtz
institute, Mainz, Germany;
6
UCB Physics, NSD LBNL, Berkeley, CA
In this presentation I will describe our labs' latest
developments in zero and ultralow field NMR spectroscopy
detected
using
atomic
magnetometers.
Using
electromagnetic coils located inside the magnetically shielded
(zero-field) volume of our instrument, we are able to supply
magnetic fields up to circa 10 gauss at the NMR sample while
87
it sits adjacent to the detector - an optically pumped Rb
vapor cell. We are able to control the magnetic fields in such
a way as to perform, for the first time, several “favourite“ highfield NMR experiments in combination with zero-field
detection: isotope-selective “high-field” pulses, correlation
(2D) spectroscopy, preparation of long-lived spin states,
hyperpolarisation transfer at level anticrossings.
Poster 456
MAS Beyond 100 kHz – A Synopsis of Technology and
Applications
1
1
1
1
Benno Knott ; David Osen ; Alex Krahn ; Armin Purea ; David
3
3
3
Bennett ; Loren B. Andreas ; Daniela Lalli ; Kevin J.
3
3
3
3
Sanders ; Andrea Bertarello ; Jan Stanek ; Diane Cala ;
3
3
2
Lyndon Emsley ; Guido Pintacuda ; Jochem Struppe ;
1
1
Sebastian Wegner ; Frank Engelke
1
2
Bruker Biospin, Rheinstetten, Germany; Bruker Biospin,
3
Billerica, MA; ENS Lyon, Lyon, France
MAS at very high spinning rates (> 100 kHz) requires
miniaturization of the MAS system to the sub-mm range of
dimensions with novel precision manufacturing techniques.
New challenges of sample loading and rotor handling arise,
and the efficient regulation of air flow for sub-mm MAS
systems must be addressed. We introduce our new 0.7 mm
MAS system enabling spinning rates above 110 kHz
transforming NMR investigations of biosolids and materials.
Notably the improved averaging of homonuclear proton-proton
couplings, e.g., in protein samples, or of paramagnetically
induced broadening, for example, in catalysts or in batteryrelated compounds, the new 0.7 mm MAS probes will open a
wide range of applications.
Page 124
Poster 457
A NQR-based Authentication System for the Non-Invasive
and Non-Destructive Authentication of Packaged
Pharmaceutical Products
Gianni Ferrante
Stelar s.r.l., Mede (Pv), Italy
The aim of this work was to develop a portable and easy-touse sensor based on NQR (nuclear quadrupolar resonance),
for customs officers and other agents of law enforcement, for
distinguishing genuine medicines from fakes without the need
to remove the medicines from their packaging or shipping box.
Compounds containing a quadrupolar nucleus can be
analyzed by NQR. Those containing nitrogen, chlorine or
bromine, sodium and potassium nuclei are particularly
suitable, which includes over 80% of all drugs.
The design and the development of a specific user-friendly,
portable instrument, for non-invasive and non-destructive
screening of packaged pharmaceutical products, which can
give the operator a rapid answer as to whether or not the
packaged product is genuine or counterfeit, is shown herein.
Poster 458
The Design of an Agilent to Bruker (A2B) Conversion Kit
for Wide-Bore Solid-State NMR Systems
1
1
2
Tony Montina ; Michael Opyr ; Jochem Struppe ;
3
David Lewis
1
2
University of Lethbridge, Lethbridge, Canada; Bruker
3
BioSpin, Billerica, MA; Revolution NMR LLC, Fort Collins, CO
The recent exit of Agilent Technologies from the NMR
business has left the global NMR community with a great deal
of concerns. One such concern is the question of how NMR
labs will continue to make use of their existing selection of
Agilent NMR probes, while still being able to upgrade their
consoles. This presentation illustrates the design elements of
an Agilent to Bruker (A2B) conversion kit for wide-bore solidstate NMR systems. This kit provides fully automated control
of both Variable Temperature and Magic Angle Spinning
functions on an Agilent/Varian probe by a Bruker console and
the TopSpin software package. Furthermore, this was
achieved with minimal hardware modifications and two
“conversion boxes” that allow for a “plug and play” solution.
Poster 459
Practical Considerations for the Application of a
Pressurized Helium Recovery System to NMR Cryostats
1
2
1
Michael Opyr ; Calvin Winter ; Tony Montina
1
2
The University of Lethbridge, Lethbridge, Canada; Quantum
Technology Corp, Squamish, Canada
This work will illustrate the operating principles of an early
model pressurized helium recovery system that has been
modified to allow for the safe recovery of helium gas from
NMR cryostats. The primary benefit of an all metal
compressor backed helium recovery system is the ability to
collect gas from helium fills without the need for both a helium
bag and gas purification. This type of system requires special
design elements in order to protect the cryostats that are not
being filled from pressure changes generated by the fill
process at a different magnet. Pressure stability is particularly
important for high resolution solution-state NMR experiments
in order to avoid T1 noise and drift.
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
Poster 460
High Resolution Solid-State Magnetic Resonance Imaging
Eric Moore; Robert Tycko
LCP, NIDDK, National Insitutes of Health, Bethesda, MD
High resolution magnetic resonance imaging offers an entirely
different imaging modality compared to optical, scanning or
electron microscopies by allowing the wealth of NMR
techniques to be applied to the image contrast problem.
Unfortunately, the applications are limited by the need for
adequate sensitivity and spatial resolution. One solution to
this problem is to apply dynamic nuclear polarization
techniques to increase the spin polarization 10-100 fold and
thereby improve the sensitivity. Following this approach to
high resolution imaging requires a custom magnetic
resonance imaging probe capable of solids imaging at
cryogenic temperatures. We have constructed such a probe
and here we report the first room-temperature images of a
solid sample produced using it.
Poster 461
NMR Detection of Tomato Paste Spoilage in 1,000 L,
Metal Lined Totes
1
2
1
Michele Martin ; Paul Giammatteo ; Michael McCarthy ;
1
Matthew Augustine
1
2
University of California, Davis, Davis, CA; Process NMR
Associates, Danbury, CT
Low field nuclear magnetic resonance (NMR) is used as a
non-invasive method for detecting spoiled tomato paste. It is
1
shown that the H T1 and T2 relaxation times change as
tomato paste spoils due to changes in viscosity and/or
changes in the concentration of paramagnetic compounds.
With the goal of developing a spoilage detector that can be
used in a tomato processing facility, a γBo = 19.5 MHz singlesided handheld NMR instrument is used. Due to the
dominance of diffusion on relaxation measurements made
with the single sided instrument, the slope of the amplitude of
a spin echo for three different delay times is used to provide a
viscosity dependent parameter that permits the differentiation
between pristine and spoiled tomatoes.
Poster 462
A Broadband Tunable System for a Single-Tuned Cryocoil
MAS-NMR Probe
1
1
2
3
Takashi Mizuno ; Mitsuru Toda ; Koji Fujioka ; K. Takegoshi ;
4
4
Yuuki Mogami ; Tadashi Shimizu
1
2
JEOL Resonance Inc., Akishima, Japan; Cryoware Inc.,
3
Tsukuba, Japan; Dept. of Chemistry, Kyoto Univ., Kyoto,
4
Japan; NIMS, Tsukuba, Japan
A cryocoil MAS-NMR probe which would be presented is
compatibly consisted both of a sample spinning system
around room-temperature and a cryogenically refrigerating
system for signal detector under low temperature under 20 K,
which results in higher S/N gain on high-resolution solid-state
NMR by attenuating thermal noise in the detector and being
increased its coil-Q. For example, the sensitivity enhancement
6
factor is 4.4 for Li. In this report, a broadband tunable system
for a single-tuned cryocoil MAS-NMR probe should like to be
illustrated. In practice, the attained tuning range is 72 MHz to
196 MHz with the 4-turn solenoid coil, and 30 MHz to 90 MHz
with the 12-turn solenoid coil.
Poster 463
Ultra-High Sensitivity in High-Resolution Relaxometry by
Using a Cryo-probe and a Fast Mechanical
Sample Shuttle Device
1, 6
2
3
Ching-Yu Chou ; Minglee Chu ; Chi-Fon Chang ; Tai-huang
4
5
1
Huang ; Angelo Guiga ; Fabien Ferrage ; Dimitrios
6
Sakellariou
1
Ecole Normale Supérieure et CNRS, UMR 7203, Paris,
2
France; Institute of Physics, Academia Sinica, Taipei,
3
Taiwan, R.O.C.; Genomics Research Center, Academia
4
Sinica, Taipei, Taiwan, R.O.C.; Institute of BioMedical
5
Science, Academia Sinica, Taipei, Taiwan, R.O.C.; CEASaclay, DSM/IRAMIS/NIMBE UMR3685, Gif-sur-Yvette,
6
France; CEA-Saclay, DSM/IRAMIS/NIMBE/LSDRM
UMR3685, Gif-sur-Yvette, France
Dynamics investigation on macromolecular systems can
greatly benefit from a sample-shuttling hardware operating on
a high field solution NMR used for measuring field-dependent
relaxation in high-resolution spectra. Recently, we have
designed a high performance fast sample-shuttling device and
installed it on various types of high field NMR spectrometers
in France and in Taiwan, including a standard solution NMR
700 MHz spectrometer equipped with a 5 mm cryoprobe
system, from which the recorded data are presented.
Benefiting from the cyroprobe detection, we acquired ultrahigh sensitivity in field cycling experiments on sub-millimolar
15
N-labeled ubiquitin. This
concentration solutions of
unprecedented high sensitivity opens a variety of biological
applications including the dynamics of intrinsically disordered
proteins and the folding/unfolding mechanisms.
Poster 464
Instrument Development for Coherence-Spectroscopy
Approach to DNP at 200 GHz
1
1
1
Ting Ann Siaw ; Alisa Leavesley ; Alicia Lund ; Arvid
2
1
1
Niemöller ; Ilia Kaminker ; Songi Han
1
Department of Chemistry, UC Santa Barbara, Santa Barbara,
2
CA; AcalNet, RWTH Aachen, Aachen, Germany
We present the development of a 7 T dynamic nuclear
polarization (DNP) and electron paramagnetic resonance
(EPR) instrument operational at liquid helium temperatures.
The instrument is powered by a dual microwave source
tunable from 193-201 GHz, mounted on a quasi-optical
microwave bridge for control, transmission, and detection of
coherent microwaves. The digital control of this microwave
bridge by Specman4EPR enables phase-sensitive pulsed and
cw or FM microwave transmission, superheterodyne detection
and synchronized NMR pulses. A home-built NMR probe is
employed to maximize versatility and robustness. We will
discuss a series of developments ranging from dual-frequency
microwave bridge design, Specman software integration of
the hardware, NMR probe design, methods for quasi optic
diagnosis, and microwave transmission performance analysis.
Poster 465
Performance Evaluation of Catheter Imaging Coils for
Endovascular MR Imaging
1, 2
1
1
Xiaoliang Zhang ; Alastair Martin ; Prasheel Lillaney ; Aaron
1
1
1
Losey ; Daniel Cooke ; Steven Hetts
1
University of California San Francisco, San Francisco, CA;
2
UC Berkeley/UCSF Joint Bioengineering Program,
San Francisco, CA
Page 125
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
In this work, we evaluate the reception sensitivity of the newly
developed transmission line catheter imaging coils through
the comparison study with conventional lumped element
catheter coil and also the body coil. The results demonstrate
significant SNR gain of the transmission line catheter coils
over the lumped elements (with twisted leads) and the body
coil at 1.5T. This SNR gain also helps enhanced imaging
coverage which is a critical factor for the miniature catheter
coils.
different approaches to shimming. We propose a scheme
where the six orientations of external hexagonal magnets are
the degrees of freedom used to shim the field. The static and
perturbative fields are described in terms of spherical
harmonics and combinatorially optimized to eliminate
inhomogeneities. While our calculations of a one-shell shim
unit give modest improvements of a factor of 10 to the ideal
HM, incorporation of error in the HM actually allows for better
improvement (factor of 25).
Poster 466
Innovative Capabilities a the EMSL User Facility to
Support the Study of Materials and Biosystems with
Advanced NMR spectroscopy
1
1
2
3
Jesse Sears ; Sarah Burton ; Nancy Isern ; Nancy Washton ;
1
1
1
Hardeep Mehta ; Michael Froehlke ; Andrew S. Lipton ; David
3
1
1
W Hoyt ; Chad Lawrence ; Patrick N Reardon ; Ryan
1
1
3
Renslow ; Eric Walter ; Karl Mueller
1
2
Battelle PNNL, Richland, WA; Environmental Molecular
3
Sciences Lab, Pacific Nort, Richland, WA; Pacific Northwest
National Laboratory, Richland, WA
The Environmental Molecular Sciences Laboratory (EMSL) is
a Department of Energy national scientific user facility, located
at Pacific Northwest National Laboratory in Richland,
Washington.The EMSL facility houses an array of scientific
equipment for research critical to national needs. The state-ofthe-art resources offered by EMSL include computation,
deposition/microfabrication, kinetics and reaction, mass
spectrometry,
microscopy,
NMR/EPR,
spectroscopy/
diffraction, and subsurface flow and transport capabilities.
Capabilities and expertise that contribute to a problemsolving, team-based research environment in areas including
materials development, catalysis, structural biology, and
metabolomics will be presented. Although special emphasis
will be placed on recent developments and upgrades in the
area of NMR spectroscopy, highlights of selected user
projects employing multiple capabilities will also be included.
Poster 468
Open-Access Automated Sample Loading from Vials:
Segmented Flow Accommodates Samples in All NMR
Solvents
Roger Kautz
Barnett Institute of Chem and Biol Analysis, Boston, MA
Automated sample loading using flow-NMR is inconvenient in
open-access facilities, where samples may be in any of the
common NMR solvents. As an alternative to flushing and repriming the pump with different deuterated solvents,
segmented flow using the fluorocarbon fluid FC-43 can load
sequential samples in dissimilar solvents. To implement
segmented flow, minimally the pump is simply filled with FC.
In practice, larger-bore (200 um) tubing supports faster
sample loading, and is resistant to clogging. Some results
with a new 50 uL (4 mm) solenoidal flow probe will be
presented. This offers only a 5x mass sensitivity advantage
over a 5 mm room-temp probe (comparable to a cryoprobe),
but samples are 0.1 mM concentration suitable for ligand
binding studies.
Poster 467
The Beginnings of a Strategy for Shimming Haibach
Magnets for NMR Spectroscopy that Profits from Material
Imperfections
1
2
3
Anna Parker ; Wasif Zia ; Bernhard Bluemich
1
2
Universiy of California, Berkeley, Berkeley, CA; ITMC,
RWTH-Aachen, Aachen, Germany;
3
RWTH Aachen University, Aachen
In the pursuit of miniaturizing NMR technology, the primary
barrier is producing a static magnetic field with sufficient
homogeneity, which must be <10 ppb for chemical analysis.
Extensive effort has produced competitive Halbach magnets
(HMs) for this purpose, but further miniaturization requires
Page 126
Poster 469
1
PCB-based H/X/Y Probe Design for MAS NMR Combines
Efficiency with Versatility
Peter L. Gor'kov; Jason Kitchen; Ilya Litvak; Ivan Hung;
William W. Brey
National High Magnetic Field Lab / FSU, Tallahassee, FL
PC boards can provide versatile and convenient building
blocks for solid-state NMR probe engineers. We present
1
electro-mechanical design of triple-resonance H/X/Y 800
MHz MAS probe that compacts most of X/Y circuit
components on two removable PCB cards. Such "tune card"
approach allows for diverse variety of X and Y isotope
configurations as well as S/N optimizations for X- or Ydetection; all done on a single probe frame. We discuss
reduction of construction costs by using PCBs, 3D-printing,
and examine strategies that improve direct detection S/N:
designing RF coils for higher magnetization transfer in multiCP experiments and reducing losses in probe isolation traps.
We will also report on construction progress of a similar 1.5
GHz MAS probe for NHMFL Series-Connected hybrid.
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
POSTERS OF MONDAY & TUESDAY SHORT TALKS
These posters should be set up on Monday and removed after poster session on Tuesday.
Abstracts for these posters appear in section for “Abstracts of Talks”
Poster 470
Studies of a 1 MDa Chaperonin in Action by Combined
NMR and EM Approaches; Guillaume Mas; Pavel Macek;
Elodie Crublet; Christine Moriscot; Schanda Paul; Schoehn
Guy; Boisbouvier Jerome; Structural Biology Institute,
Grenoble, France
Poster 471
Ligand-Protein Screening by Long-Lived States of
1
1
Fluorine-19 Nuclei; Roberto Buratto ; Daniele Mammoli ;
1
1, 2
1
Aurélien Bornet ; Estel Canet ; Basile Vuichoud ; Jonas
1
1
1, 2 1
Milani ; Sami Jannin ; Geoffrey Bodenhausen ; EPFL,
2
Lausanne, Switzerland; ENS, Paris, France
Poster 472
Real-Time Monitoring of Enzymatic Reactions in Living
Cells by NMR and Its Applications in Drug Discovery; Jun
Hu; AstraZeneca, Waltham, MA
Poster 473
High Resolution Solid-State NMR of Highly Radioactive
Materials: A new insight into the 5f-chemistry of
paramagnetic compounds; Laura Martel; Chris Selfslag;
Joseph Somers; JRC-ITU, Eggenstein Leopoldshafen,
Germany
Poster 474
Dynamic Nuclear Polarization enhanced Solid State NMR
of Insensitive Nuclei: Oxygen-17 at Natural Abundance
and Low-gamma Yttrium-89; Frédéric Blanc; University of
Liverpool, Liverpool, UK
Poster 475
Mg NMR Studies of Mg-ion Battery Materials; Hao
1
1
3
Wang ; Danielle Proffit ; Cheon Jung Kim ; Premkumar
1
2
2
3
Senguttuvan ; Victor Duffort ; Linda Nazar ; Jordi Cabana ;
1
1
1 1
Anthony Burrell ; John Vaughey ; Baris Key ; Argonne
2
National Laboratory, Lemont, IL; University of Waterloo,
3
Waterloo, Canada; University of Illinois at Chicago, Chicago,
IL
25
Poster 476
Structure of an RNA by Solid-State NMR; Alexander
1
1
2
Marchanka ; Bernd Simon ; Gerhard Althoff ; Teresa
1 1
2
Carlomagno ; EMBL, Heidelberg, Germany; Bruker BioSpin,
Rheinstetten, Germany
Poster 477
The Capsid Model of Intact M13 Bacteriophage from MAS
NMR and Rosetta Modeling: a Quadrupled Hydrophobic
1
2
Viral Packing Epitope; Omry Morag ; Nikolaos Sgourakis ;
1
3
1 1
Gili Abramov ; David Baker ; Amir Goldbourt ; Tel Aviv
2
University, Tel Aviv, Israel; NIDDK, NIH, Bethesda, MR;
3
University of Washington, Seattle, WA
2
Analytiques, Lyon, France; Dept of Biosciences, Milano, Italy;
3
4
Dept of Molecular Medicine, Pavia, Italy; Univ College
5
London, London, UK; Ecole Polytechnique Federale de
Lausanne, Lausanne, Switzerland
Poster 479
F NMR Reveals Multiple Conformations at the Dimer
Interface of the Non-Structural Protein 1 Effector Domain
1
1
from Influenza A Virus; James Aramini ; Keith Hamilton ; Li1
1
2
2
Chung Ma ; G.V.T. Swapna ; Paul Leonard ; John Ladbury ;
3
1 1
Robert Krug ; Gaetano Montelione ; CABM, Rutgers
2
University, Piscataway, NJ; University of Texas MD
Anderson Center, Houston, TX;
3
University of Texas, Austin, TX
19
Poster 480
HOBS: Broadband Homonuclear Decoupled BandSelective NMR Experiments with Full Sensitivity; Laura
Castañar Acedo; Albert Vigili; Teodor Parella; Universitat
Autónoma Barcelona, Cerdanyola Del Vallés,
Barcelona, Spain
Poster 481
Probing the Structural and Dynamical Effects of the
Charged Residues of the TZF Domain of TIS11d; Brittany
Morgan; Laura Deveau; Francesca Massi; University of
Massachusetts, Worcester, MA
Poster 482
A Statistical Torsion Angle Potential Improves the Quality
of NMR-based RNA Structures; Guillermo Bermejo; Marius
Clore; Charles Schwieters; National Institutes of Health,
Bethesda, MD
Poster 483
Dynamic in vivo Free Radical Imaging with Overhauser1, 2
3
Enhanced MRI; Mathieu Sarracanie ; Fanny Herisson ;
1, 2
1, 4
3, 5
Najat Salameh ; David Waddington ; Cenk Ayata ;
1, 5 1
Matthew Rosen ; MGH/A.A. Martinos Center for Biomedical
2
Imaging, Charlestown, MA; Department of Physics, Harvard
3
University, Cambridge, MA; Neurovascular Research Lab,
4
MGH, Charlestown, MA; School of Physics, University of
5
Sydney, Sydney, Australia; Harvard Medical School,
Boston, MA
Poster 484
Group Sparse Reconstruction of Highly Undersampled
Echo Planar Correlated Spectroscopic Imaging Scan:
Application to Human Calf; Neil Wilson; Brian Burns; Zohaib
Iqbal; M. Albert Thomas; UCLA, Los Angeles, CA
Poster 478
Probing the Mechanism of Fibril Formation in D76N β-2Microglobulin with Ultra-Fast Magic-Angle Spinning;
1
1
Tanguy Le Marchand ; Loren Andreas ; Emeline Barbet1
1
1
2
Massin ; Michael Knight ; Hugh Dannatt ; Stefano Ricagno ;
2
3
4
Martino Bolognesi ; Sofia Giorgetti ; Vittorio Bellotti ; Lyndon
5
1 1
Emsley ; Guido Pintacuda ; Institut des Sciences
Page 127
POSTERS
All posters should be set up Monday morning and removed at 3:45 PM on Thursday. Be sure to use the poster space number printed here.
Authors of odd-number posters present on Monday and Wednesday. Even-number posters present on Tuesday and Thursday.
POSTERS OF WEDNESDAY & THURSDAY SHORT TALKS
These posters should be set up on Wednesday and removed after poster session on Thursday.
Abstracts for these posters appear in section for “Abstracts of Talks”
Poster 470
Local and Bulk 13C Hyperpolarization in NV-Centered
Diamonds at Variable Fields and Orientations; Gonzalo
1
1
Agustin Alvarez ; Christian Oliver Bretschneider ; Ran
2
2
3
4
Fischer ; Paz London ; Hisao Kanda ; Shinobu Onoda ;
5
2
1 1
Junichi Isoya ; David Gershoni ; Lucio Frydman ; Weizmann
2
Institute of Science, Rehovot, Israel; Technion, Haifa, Israel;
3
National Institute for Materials Science, Tsukuba, Japan;
4
5
Japan Atomic Energy Agency, Takasaki, Japan; University
of Tsukuba, Tsukuba, Japan
Poster 471
Room-Temperature in situ Nuclear Spin Hyperpolarization
from Optically-Pumped Nitrogen Vacancy Centers in
1, 2
1, 2
Diamond; Jonathan P King ; Keunhong Jeong ;
1, 2
1, 2
1
Christophoros Vassiliou ; Chang Shin ; Ralph Page ;
1, 2
1
1, 2 1
Claudia Avalos ; Haijing Wang ; Alex Pines ; Department
2
of Chemistry, UC Berkeley, CA; Materials Sciences Division,
LBNL, Berkeley, CA
Poster 472
Transient Complexes Observed by Paramagnetic
Ntr
Relaxation Enhancement between Enzyme 1 and NPr
Prevent Crossover between Phosphorylation Pathways;
1
2
Madeleine Strickland ; Ann Marie Stanley ; Guangshun
3
4
1
1
Wang ; Susan Buchanan ; Alan Peterkofsky ; Nico Tjandra ;
1
2
NHLBI, NIH, Bethesda, MD; NIGMS, NIH, Bethesda, MD;
3
Nebraska Medical Center, Omaha, NE;
4
NIDDK, NIH, Bethesda, MD
Poster 473
NMR to Measure Molecular-Level Curvature of
Membranes by Proteins and Lipids; Adrian Draney; Sean
Smrt; Justin Lorieau; University of Illinois, Chicago, IL
Poster 474
A Robust Suite of Fast and Ultrafast Methods for In Vivo
Spectroscopy Imaging of pre-Targeted Metabolic Peaks;
1
1, 2
1, 3
Amir Seginer ; Zhiyong Zhang ; Noam Shemesh ; Rita
1, 4
1 1
Schmidt ; Lucio Frydman ; Weizmann Institute, Rehovot,
2
3
Israel; Xiamen University, Xiamen, China; Champalimaud
4
Centre for the Unknown, Lisbon, Portugal; Leiden University
Medical Center, Leiden, The Netherlands
Poster 475
Isolated Amide Proton CEST Contrast at 7 T Correlates
with Contrast-Enhanced T1w-images of Tumor Patients;
1
1
1
Johannes Windschuh ; Steffen Goerke ; Jan-Eric Meissner ;
2
1
1 1
Alexander Radbruch ; Peter Bachert ; Moritz Zaiss ; German
2
Cancer Research Center, Heidelberg, Germany; University of
Heidelberg Medical Center, Heidelberg, Germany
Poster 476
Magnetic Resonance Imaging of Metabolically Labeled
Glycans using Hyper-CEST Xenon Biosensors in a LiveCell Bioreactor; Christopher Witte; Honor Rose; Vera Martos
Riaño; Stefan Reinke; Stefan Klippel; Christian Hackenberger;
Leif Schröder; Leibniz-Institut für Molekulare Pharmakologie,
Berlin, Germany
Page 128
Poster 477
Hybrid Polarizing Solids for Pure Hyperpolarized Liquids
through Dissolution Dynamic Nuclear Polarization; David
1
2
2
2
Gajan ; Aurélien Bornet ; Basile Vuichoud ; Jonas Milani ;
3
4
4
Roberto Melzi ; Henri A. van Kalkerendd ; Laurent Veyre ;
4
5
5
Chloé Thieuleux ; Matthew P. Conley ; Wolfram R. Gruning ;
5
1
5
Martin Schwarzwalder ; Anne Lesage ; Christophe Copéret ;
2, 6
2
2
Geoffrey Bodenhausen ; Lyndon Emsley ; Sami Jannin ;
1
2
ENS Lyon, Villeurbanne, France; EPFL, Lausanne,
3
4
Switzerland; Bruker Italia S.r.l, Milano, Italy; Université de
5
Lyon, Lyon, France; ETHZ, Zurich, Switzerland;
6
ENS, Paris, France
Poster 478
Insights into DNP Mechanisms from Localized Biradicals
in the Dilute Limit; Rivkah Rogawski; Ivan Sergeyev;
Yongjun Li; Virginia Cornish; Ann McDermott;
Columbia University, New York, NY
Poster 479
In-situ Rapid Melt DNP and Supercritical Overhauser
DNP, New Approaches towards Inline 1H NMR Detection
of Low Concentration Metabolites in microfluidic flow;
Jan Van Bentum; Manvendra Sharma; Gerrit Janssen; Jim
Leggett; Michael Tayler; Bas van Meerten; Arno Kentgens;
IMM, Radboud University, Nijmegen, Netherlands
Poster 480
A Revised NNLS Approach to High-Resolution NMR
1
2 1
Relaxometry; Robert J. Klingler ; Klaus Woelk ; Argonne
2
National Laboratory, Argonne, IL; Missouri S&T, Rolla, MO
Poster 481
Line-Broadening in Low Temperature Solid-State NMR
1
1
Spectra of Fibrils; Thomas Bauer ; Claudio Dotta ; Livia
1
1
1
1
Balacescu ; Julia Gath ; Andreas Hunkeler ; Matthias Ernst ;
2
1 1
Anja Böckmann ; Beat Meier ; ETH Zurich, Zurich,
2
Switzerland; IBCP-CNRS, Lyon, France
Poster 482
15
Catalytic Roles of βLys87 in Tryptophan Synthase: N
Solid State NMR Studies; Bethany G. Caulkins; Chen Yang;
Michael F. Dunn; Leonard J. Mueller;
Univ. of California Riverside, CA
Poster 483
Reclaiming Resolution in DNP-SSNMR: Assignments and
Distances from Higher-Dimensional Experiments; Ivan
1
2
3
4
Sergeyev ; Boris Itin ; Rivkah Rogawski ; Guohua Lv ; David
4
3 1
Eliezer ; Ann Mcdermott ; Columbia Univ. / New York
2
Structural Biology, New York, New York; New York Structural
3
Biology Center, New York, NY; Columbia Univ., New York,
4
New York; Weill Cornell Medical College, New York, NY
Poster 484
1.02 GHz LTS/HTS NMR: I. Development to Overcome the
1
Limitation of Magnetic Field Strength; Masato Takahashi ;
2
2
2
1
G. Nishijima ; S. Matsumoto ; K. Hashi ; S. Iguchi ; Y.
1
1
3
3
4
Yanagisawa ; H. Maeda ; T. Miki ; K. Saito ; R. Tanaka ; T.
4
4
4
2
2
Nemoto ; T. Miyamoto ; H. Suematsu ; T. Noguchi ; S. Ohki ;
2
2 1
A. Goto ; T. Shimizu ; RIKEN CLST, Yokohama, Japan
INDEX OF AUTHORS
Abergel, Daniel ............................ Poster 362
Abhyankar, Nandita ..................... Poster 420
Abramov, Gili ..................... TOA 10:00-10:15
Acedo, Jeella Z. ........................... Poster 053
Ackerman, Jerome L. ................... Poster 181
Ackermann, Rose ........................ Poster 058
Ackerstaff, Ellen........................... Poster 355
Adam, Klaus-Peter ....................... Poster 303
Adams, Ralph W. ......................... Poster 326
Agard, David ................................ Poster 068
Agarwal, Vipin .............................. Poster 148
Aggarwal, Aneel K. ...................... Poster 130
Ahn, Hee-Chul .............................. Poster 050
Ahn, Jinwoo ........................ TOA 08:30-08:55
Ahola, Susanna ............................ Poster 231
Aitken, Bruce................................ Poster 119
Ajoy, Ashok .................................. Poster 133
Akbey, Umit .................................. Poster 083
Akinfaderin, Adewale ................... Poster 262
Akinfaderin, Adewale ................... Poster 255
Alam, Todd M. .............................. Poster 386
Alaniva, Nicholas.......................... Poster 274
Alaparthi, Rajasri ......................... Poster 365
Albert, Brice ................................. Poster 274
Alkan, Fahri ........................... MOE 4:25-4:50
Al-Kaysi, Rabih ............................ Poster 398
Allain, Frederic H.-T. ......... MOB 11:10-11:35
Almeida, Fabio ............................. Poster 059
Almeida, Fabio ............................. Poster 141
Almeida, Fabio ............................. Poster 165
Alonso Valdesueiro, Javier . ThOE 5:15-5:30
Althoff, Gerhard ................. TOA 09:45-10:00
Alvarado, Luigi ............................. Poster 029
Alvarez, Gonzalo Agustin ............. Poster 179
Alvarez, Gonzalo Agustin ............. Poster 213
Alvarez, Gonzalo Agustin ..WOA 09:45-10:00
Alvarez, Gonzalo Augustin ........... Poster 249
Alvarez, Gonzalo Augustin ........... Poster 250
Alves, Marina ............................... Poster 343
Amassian, Aram........................... Poster 401
Ambeskovic, Mirela ..................... Poster 361
Amero, Carlos .............................. Poster 010
Ames, James................................ Poster 045
Ames, James B. ........................... Poster 329
Amin, Samrat A. ........................... Poster 407
Amoureux, Jean Paul................... Poster 090
Amoureux, Jean Paul................... Poster 102
Anastácio Alves, Luiz .................. Poster 062
Andolina, Christopher .................. Poster 391
Andreas, Loren .................. TOB 12:00-12:15
Andreas, Loren B. ........................ Poster 108
Andreas, Loren B. ........................ Poster 456
Anthony, Drake ............................ Poster 275
Antignani, Antonella..................... Poster 031
Antonietti, Markus........................ Poster 403
Arai, Hajime .................................. Poster 413
Aramini, James .................. TOB 12:15-12:30
Arbogast, Luke ............................ Poster 066
Arbogast, Luke ............................ Poster 337
Arcos, Daniel........................ ThOE 5:45-6:00
Aronson, Matthew ........................ Poster 402
Arseneault, Geneviève................. Poster 026
Arshava, Boris....................... MOD 5:15-5:30
Arthanari, Haribabu...................... Poster 055
Asakura, Katsuo........................... Poster 296
Asam, Claudia .............................. Poster 059
Atreya, Hanudatta Sastry ............. Poster 339
Aubert, Guy .......................... ThOE 5:15-5:30
Aucoin, Darryl ...................... TOA 08:55-9:20
Auger, Michèle ............................. Poster 071
Augustine, Matthew ..................... Poster 329
Augustine, Matthew .....................Poster 418
Augustine, Matthew .....................Poster 461
Aussenac, Fabien ........................Poster 268
Aussenac, Fabien ........................Poster 229
Avalos, Claudia ............................Poster 226
Avalos, Claudia ................ WOA 10:00-10:15
Awschalom, D. D. ........................Poster 221
Awschalom, David .......................Poster 222
Axtman, Alison .............................Poster 317
Ayata, Cenk ............................TOE 5:05-5:20
Aycock-Rizzo, Halley ...................Poster 431
Azurmendi, Hugo .........................Poster 048
Baba, Shahid ................................Poster 205
Babcock, Earl ...............................Poster 230
Bachert, Peter ..............................Poster 186
Bachert, Peter ..............................Poster 196
Bachert, Peter ..............................Poster 194
Bachert, Peter ..............................Poster 176
Bachert, Peter ..............................Poster 188
Bachert, Peter ..................ThOA 09:30-09:50
Bacon, Paul ..................................Poster 348
Badilita, Vlad ................................Poster 439
Bajaj, Vikram ................................Poster 226
Bajaj, Vikram S. ............................Poster 220
Bajakian, Thalia............................Poster 081
Bajakian, Thalia............................Poster 082
Baker, David .......................TOA 10:00-10:15
Baker, David .......................... TOD 5:05-5:20
Balacescu, Livia .................. ThOD 5:15-5:30
Balasubramanian, Mahalingam ...Poster 415
Baldus, Marc ................................Poster 244
Baltisberger, Jay H ......................Poster 385
Baltusis, Laima ............................Poster 191
Balzan, Riccardo ..........................Poster 300
Bame, Jessica ..............................Poster 284
Banan, Guita.................................Poster 449
Banigan, James ...........................Poster 098
Banks, Benjamin ..........................Poster 195
Bao, Xinhe ....................................Poster 381
Bao, Xinhe ....................................Poster 380
Baptista, Diego.............................Poster 032
Barbar, Elisar................................Poster 001
Barbet-Massin, Emeline ...............Poster 073
Barbet-Massin, Emeline ..... TOB 12:00-12:15
Bardeen, Christopher ...................Poster 398
Barkiy, Danila ...............................Poster 246
Barlow, Michael J. .......................Poster 272
Barlow, Michael J. .......................Poster 247
Barlow, Michael J. .......................Poster 275
Barnes, Alexander ........................Poster 274
Barnes, Alexander ........................Poster 317
Barrett, Sean ................................Poster 161
Barrett, Sean ................................Poster 217
Barrett, Sean .................... WOC 12:00-12:15
Barskiy, Danila .............................Poster 235
Barth, Dominique..........................Poster 419
Bassil, Bassem.............................Poster 412
Batel, Michael ...................ThOB 11:10-11:35
Batista, Aline ................................Poster 059
Battistel, Marcos ..........................Poster 048
Bauer, Thomas .................... ThOD 5:15-5:30
Bax, Ad .........................................Poster 003
Bax, Ad .........................................Poster 127
Bayley, Paul M. ............................Poster 375
Bayro, Marvin ...............................Poster 114
Bearden, Dan ...............................Poster 427
Beaujuge, Pierre ..........................Poster 401
Becette, Owen ..............................Poster 029
Bechmann, Matthias ....................Poster 215
Becker, Johanna ..........................Poster 325
Becker, Johanna ..........................Poster 318
Program Code: M, T, W, Th, F = Day
O = Oral Time
Becker, Stefan ............................. Poster 017
Becker, Stefan ............................. Poster 124
Becker, Stefan ..................... ThOD 4:50-5:15
Becker, Stefan ....................... TOD 5:05-5:20
Beckmann, Jens.......................... Poster 412
Beckmann, Roland ...................... Poster 073
Bednarek, Elzbieta ...................... Poster 137
Bednarek, Elzbieta ...................... Poster 340
Bej, Aritra ..................................... Poster 123
Belenky, Marina........................... Poster 087
Bellanger, Jean-Jacques ............. Poster 175
Bellotti, Vittorio .................. TOB 12:00-12:15
Bennati, Marina ................ WOA 08:55-09:20
Bennett, David ............................. Poster 456
Berkamp, Sabrina........................ Poster 115
Berkson, Zachariah ..................... Poster 400
Bermejo, Guillermo ................ TOD 5:35-5:50
Bermel, Wolfgang ........................ Poster 328
Bernèche, Simon ......................... Poster 150
Berruyer, Pierrick ........................ Poster 293
Berruyer, Pierrick ........................ Poster 379
Bertarello, Andrea ....................... Poster 108
Bertarello, Andrea ....................... Poster 456
Beuf, Olivier ................................. Poster 201
Bezsonova, Irina ......................... Poster 021
Bhatnagar, Aruni ......................... Poster 205
Bhattacharya, Pratip ................... Poster 358
Bhattacharya, Pratip ................... Poster 366
Bhunia, Anirban ........................... Poster 034
Bierma, Jan ................................. Poster 028
Bignucolo, Olivier ........................ Poster 150
Bihan, Dominique ................ ThOD 4:25-4:50
Billeter, Martin ............................. Poster 165
Binder, Martin .............................. Poster 016
Bird, Mark D. ............................... Poster 452
Bischof, John .............................. Poster 187
Blackledge, Martin....................... Poster 129
Blanc, Frédéric ......................MOE 5:30-5:45
Blanchard, John .......................... Poster 227
Blanchard, John W ...................... Poster 220
Block, Robert ............................... Poster 421
Bluemich, Bernhard..................... Poster 282
Bluemich, Bernhard..................... Poster 467
Bluemler, Peter ........................... Poster 230
Bluemler, Peter ........................... Poster 232
Bluemler, Peter ................ WOC 10:45-11:10
Blum, Robert ............................... Poster 161
Blum, Robert ............................... Poster 217
Blümich, Bernhard....................... Poster 266
Blümich, Bernhard....................... Poster 267
Boakye, Maxwell .......................... Poster 206
Bocian, Wojciech ......................... Poster 137
Bocian, Wojciech ......................... Poster 340
Böckmann, Anja .................. ThOD 5:15-5:30
Bodenhausen, Geoffrey ....... MOD 5:30-5:45
Bodenhausen, Geoffrey .............. Poster 009
Bodenhausen, Geoffrey .............. Poster 130
Bodenhausen, Geoffrey .............. Poster 139
Bodenhausen, Geoffrey .............. Poster 236
Bodenhausen, Geoffrey .............. Poster 362
Bodenhausen, Geoffrey .............. Poster 384
Bodenhausen, Geoffrey .. ThOB 11:35-11:50
Boehme, Christoph .............. ThOE 4:25-4:50
Boele, Thomas............................. Poster 264
Boero, Giovanni ........................... Poster 251
Boisseau, Renaud ....................... Poster 277
Bok, Robert............................ TOE 4:50-5:05
Bolognesi, Martino ............ TOB 12:00-12:15
Boons, Geert-Jan ........................ Poster 030
Boons, Geert-Jan ........................ Poster 025
Bordonali, Lorenzo ...................... Poster 433
Poster is followed by board space.
Page 129
INDEX OF AUTHORS
Byrd, R. Andrew .................FOA 10:00-10:15
Bornet, Aurélien .................... MOD 5:30-5:45
Byrd, R. Andrew ...........................Poster 152
Bornet, Aurélien ........................... Poster 236
Cabana, Jordi ........................ MOE 5:45-6:30
Bornet, Aurélien ........................... Poster 362
Cabella, Claudia ...........................Poster 271
Bornet, Aurélien ........................... Poster 384
Cadars, Sylvian ............................Poster 400
Bornet, Aurélien ............... ThOB 11:35-11:50
Cai, Qing .......................................Poster 079
Bouchard, Jill ..................... TOB 10:45-11:10
Cala, Diane ...................................Poster 108
Bouchard, Louis-S. ...................... Poster 202
Cala, Diane ...................................Poster 456
Bouhrara, Mustapha .................... Poster 204
Calabro, David..............................Poster 408
Boujtita, Mohammed .................... Poster 277
Caldarelli, Stefano ............. TOC 12:00-12:15
Bounds, Richard .......................... Poster 373
Callon, Morgane .................TOB 11:10-11:35
Boutis, Gregory ............................ Poster 078
Camaioni, Donald M .....................Poster 377
Boutis, Gregory ............................ Poster 128
Can, Thach ...................................Poster 087
Boutis, Gregory S......................... Poster 224
Can, Thach ...................................Poster 253
Boutis, Gregory S......................... Poster 218
Canet, Estel ...........................MOD 5:30-5:45
Bowers, Clifford R .............. FOB 11:10-11:35
Canet, Estel ..................................Poster 009
Bowers, Clifford R ........................ Poster 258
Cao, Chunling ...............................Poster 051
Bowers, Clifford R ........................ Poster 252
Capozzi, Andrea ...........................Poster 203
Bowyer, Paul ........................ ThOE 4:00-4:25
Capozzi, Andrea ...........................Poster 251
Boyle, David ................................. Poster 354
Cappellaro, Paola.........................Poster 133
Branca, Rosa Tamara .................. Poster 185
Cappellaro, Paola.........................Poster 224
Branca, Rosa Tamara .................. Poster 239
Carel, Clement ..............................Poster 103
Bräse, Stefan................................ Poster 328
Carlier, Ludovic ............................Poster 130
Braun, Manuel .............................. Poster 232
Carlier, Paul .................................Poster 323
Bremmer, Marc .................... ThOE 5:45-6:00
Carlomagno, Teresa ....................Poster 022
Brender, Jeffrey ........................... Poster 034
Carlomagno, Teresa .......... TOA 09:45-10:00
Bretschneider, Christian Oliver .... Poster 250
Carpenter, Keri L.H. .....................Poster 352
Bretschneider, Christian Oliver .... Poster 249
Bretschneider, Christian OliverWOA 09:45-10:00Carpenter, T. Adrian .....................Poster 352
Carravetta, Marina........................Poster 072
Brey, William ................................ Poster 449
Carravetta, Marina........................Poster 075
Brey, William W. ........................... Poster 262
Carravetta, Marina........................Poster 373
Brey, William W. ........................... Poster 452
Brey, William W. ........................... Poster 442
Carvajal, Lucas.............................Poster 189
Brey, William W. ........................... Poster 469
Casagrande, Fabio .......................Poster 016
Brigaud, Thierry ........................... Poster 039
Casano, Gilles ..............................Poster 229
Casano, Gilles ..............................Poster 263
Brinson, Robert ............................ Poster 337
Case, David ..................................Poster 145
Brooks, Roger ......................ThOD 4:25-4:50
Case, David ..................... ThOC 10:45-11:10
Brougham, Dermot ...................... Poster 241
Case, David ........................TOB 10:45-11:10
Brow, David A. ............................. Poster 043
Casey, Thomas.............................Poster 423
Brown, Leonid .............................. Poster 116
Cassani, Julia ...............................Poster 327
Brown, Leonid .............................. Poster 086
Castañar Acedo, Laura ..... TOC 12:15-12:30
Brown, Steven Paul...................... Poster 285
Castellino, Francis J.....................Poster 005
Brubaker, William D. .................... Poster 131
Catalano, Jaclyn .................... MOE 4:25-4:50
Brüll, R ......................................... Poster 369
Caulkins, Bethany G. ...................Poster 040
Bruno, Thomas ............................ Poster 027
Caulkins, Bethany G. .......... ThOD 5:30-5:45
Bruno, Thomas ............................ Poster 302
Cavagnero, Silvia .........................Poster 257
Buchanan, Susan..............WOB 12:00-12:15
Cegelski, Lynette..........................Poster 099
Budker, Dmitry ............................. Poster 228
Cegelski, Lynette..........................Poster 109
Budker, Dmitry ............................. Poster 227
Cegelski, Lynette..........................Poster 097
Budker, Dmitry ............................. Poster 220
Cegelski, Lynette..........................Poster 317
Budker, Dmitry ............................. Poster 455
Celestine, Chi ...............................Poster 006
Buevich, Alexei ............................ Poster 304
Centeno, Silvia ...................... MOE 4:25-4:50
Bugni, Tim .................................... Poster 299
Cervantes, Silvia ..........................Poster 081
Bulatowicz, Michael ......... WOC 11:35-12:00
Cervantes Cortes, Silvia ..............Poster 082
Bull, Stephanie ............................. Poster 284
Chabot, Philippe ...........................Poster 026
Burant, Alex ................................. Poster 185
Chan, Shelby ......................... MOE 4:25-4:50
Burant, Alex ................................. Poster 239
Chandra, Kousik ...........................Poster 215
Buratto, Roberto.................... MOD 5:30-5:45
Chandra, Kousik ...........................Poster 339
Bürck, Jochen .............................. Poster 071
Chang, Chi-Fon ............................Poster 463
Burger, Jessica ............................ Poster 027
Chang, Hee Jung.............. WOC 12:15-12:30
Burgess, Stephen ........................ Poster 432
Chang, Yan ..................................Poster 170
Burkart, Michael D. ...................... Poster 065
Chao, Fa-An .......................FOA 10:00-10:15
Burmann, Björn M. ............. TOB 11:10-11:35
Charlier, Cyril ...............................Poster 130
Burns, Brian ........................... TOE 5:35-5:50
Charlier, Cyril ...............................Poster 139
Burns, Darcy C. ............................ Poster 306
Charnock, Gareth .........................Poster 146
Burrell, Anthony .................... MOE 5:45-6:30
Burton, Sarah............................... Poster 466
Chase, Lawrence ..........................Poster 242
Burz, David ................................... Poster 019
Chatterjee, Subhasish ..................Poster 079
Bussy, Ugo................................... Poster 277
Chaudhari, Sachin Rama .............Poster 276
Chaume, Grégory .........................Poster 039
Butcher, Samuel E. ...................... Poster 043
Chauvel, P....................................Poster 369
Butts, Craig P ............................... Poster 284
Cheatham, Steve F.......................Poster 278
Byeon, In-Ja ....................... TOA 08:30-08:55
Program Code: M, T, W, Th, F = Day
Page 130
O = Oral Time
Chekmenev, Eduard .................... Poster 260
Chekmenev, Eduard .................... Poster 272
Chekmenev, Eduard .................... Poster 273
Chekmenev, Eduard .................... Poster 247
Chekmenev, Eduard .................... Poster 235
Chekmenev, Eduard .................... Poster 243
Chekmenev, Eduard .................... Poster 275
Chekmenev, Eduard Y ................ Poster 246
Chen, Banghao ............................ Poster 412
Chen, Bin ..................................... Poster 029
Chen, Cheng-Yu .......................... Poster 030
Chen, Junzheng ........................... Poster 416
Chen, Qiaoyan ............................. Poster 426
Chen, Shizhen ............................. Poster 338
Chen, Vincent .............................. Poster 160
Chen, Xian ................................... Poster 453
Chen, Yu-Wen ............................. Poster 183
Chen, Yu-Wen ............................. Poster 182
Chen, Yu-Wen ............................. Poster 436
Chen, Zhong ................................ Poster 295
Cheneval, Olivier ......................... Poster 076
Cheng, Chia-Hau ......................... Poster 182
Cheng, Ren-Hao .......................... Poster 382
Cheng, Ren-Hao .......................... Poster 405
Cheng, Tian ................................. Poster 251
Cheng, Wei ........................ FOB 11:10-11:35
Cheng, Wei .................................. Poster 252
Cherry, Brian ............................... Poster 407
Chi, Celestine........................ MOD 4:25-4:50
Chi, Lingyu ................................... Poster 421
Chialvo, Cesar ............................. Poster 424
Chmelka, Brad ............................. Poster 402
Chmelka, Brad ............................. Poster 396
Chmelka, Bradley ........................ Poster 403
Chmelka, Bradley ........................ Poster 400
Chmelka, Bradley ........................ Poster 401
Chmelka, Bradley F. .................... Poster 399
Choi, Eric ..................................... Poster 274
Choi, Eun-Sang ........................... Poster 420
Choi, Seo-Ree ............................. Poster 135
Choi, Yong-Geun ......................... Poster 013
Chou, Ching-Yu ........................... Poster 130
Chou, Ching-Yu ........................... Poster 463
Chow, Wing Ying ................. ThOD 4:25-4:50
Christensen, Niels J. ................... Poster 320
Christophe, Copéret .................... Poster 263
Chu, Minglee................................ Poster 463
Chu, Shidong ............................... Poster 342
Chu, Shidong ............................... Poster 341
Cizmeciyan, Deniz....................... Poster 292
Clark, Mallory ............................... Poster 051
Clark, Matthew A. ........................ Poster 136
Clark, Sarah................................. Poster 001
Claytor, Kevin .............................. Poster 301
Clendinen, Chaevien ................... Poster 357
Clore, Marius ......................... TOD 5:35-5:50
Cobas, Carlos .............................. Poster 162
Codina, Anna ............................... Poster 316
Coffey, Aaron............................... Poster 247
Coffey, Aaron............................... Poster 243
Coffey, Aaron............................... Poster 272
Coffey, Aaron............................... Poster 273
Coffey, Aaron............................... Poster 246
Coffey, Aaron............................... Poster 275
Coffey, Aaron............................... Poster 260
Cohen, Ouri ................................. Poster 178
Cohen, Ouri ................................. Poster 181
Collier, Kelsey ............................. Poster 445
Collins, James ............................. Poster 350
Colombo, Sonia........................... Poster 271
Comment, Arnaud ....................... Poster 203
Poster is followed by board space.
INDEX OF AUTHORS
Comment, Arnaud ........................ Poster 180
Comment, Arnaud ........................ Poster 251
Comment, Arnaud .................. TOE 4:25-4:50
Cong, R ........................................ Poster 369
Conley, Matthew........................... Poster 379
Conley, Matthew P. .......... ThOB 11:35-11:50
Conrad Soria, Maria..................... Poster 081
Conrad Soria, Maria..................... Poster 082
Conradi, Mark S. .......................... Poster 397
Cooke, Daniel ............................... Poster 465
Cooley, Clarissa Zimmerman ....... Poster 450
Coote, Paul................................... Poster 055
Copéret, Christophe ..................... Poster 379
Copéret, Christophe ......... ThOB 11:35-11:50
Cornilescu, Gabriel ...................... Poster 043
Cornilescu, Gabriel ...................... Poster 160
Cornish, Virginia............... ThOB 12:05-12:20
Cortes, Patricia............................. Poster 130
Corzilius, Björn .................WOA 08:30-08:55
Cothran, Vince ..................... ThOE 5:45-6:00
Cousin, Samuel ............................ Poster 139
Craft, D. Levi ................................ Poster 154
Craigen, Kimberley ....................... Poster 104
Craik, David .................................. Poster 076
Cramer, Christopher J. ................. Poster 245
Cramer, Steven ............................ Poster 023
Crane, Ben ................................... Poster 066
Cross, Timothy A. ......................... Poster 100
Cross, Timothy A. ......................... Poster 452
Crouch, Ronald C......................... Poster 306
Croy, Jason .................................. Poster 415
Crublet, Elodie .................. MOB 12:00-12:15
Cyr, Normand ............................... Poster 026
d'Auvergne, Edward .................... Poster 280
Daebel, Venita .............................. Poster 073
Daffe, Mamadou ........................... Poster 103
Dalal, Naresh ................................ Poster 412
Dalal, Naresh ................................ Poster 420
Dalby, Kevin .......................... MOD 5:15-5:30
Dama, Murali ................................ Poster 314
Damron, Joshua ........................... Poster 085
Damron, Joshua ........................... Poster 288
Danieli, Ernesto ............................ Poster 282
Dannatt, Hugh .................... TOB 12:00-12:15
Dantu, Sarath Chandra ................. Poster 120
Dao, Phuong ................................. Poster 121
Dao, Phuong ................................. Poster 269
Das, Bibhuti .................................. Poster 115
Das, Bibhuti .................................. Poster 113
Das, Jitendra K. ............................ Poster 123
Dashti, Hesam .............................. Poster 160
Dastmalchi, Keyvan ..................... Poster 079
David, Bennett .............................. Poster 414
Davidowski, Stephen K. ............... Poster 407
Davis, Jeffrey................................ Poster 285
Davis, Michael .............................. Poster 385
Daviso, Eugenio ........................... Poster 087
Day, Iain ....................................... Poster 367
Dayie, Kwaku................................ Poster 029
De Angelis, Anna ......................... Poster 115
De Angelis, Anna ......................... Poster 105
de Magalhães, Mariana ................ Poster 141
de Mattos Zeri, Ana Carolina ....... Poster 052
de Oliveira Silveira, Juliano ......... Poster 051
de Visser, Ries ............................. Poster 346
Debelouchina, Galia .................... Poster 117
Deborde, Catherine ...................... Poster 345
Deelchand, Dinesh ....................... Poster 174
DeGroot, W .................................. Poster 369
Deguchi, Kenzo............................ Poster 454
DeKoster, Greg ............................ Poster 134
Dekoster, Greg ................. WOB 11:35-12:00
Del Rio-Portilla, Federico .............Poster 060
Delaney, Sean ..............................Poster 310
Delsuc, Marc-André ......................Poster 298
Demange, Pascal .........................Poster 103
Demers, Jean-Philippe .......... TOD 5:05-5:20
DeMott, Christopher......................Poster 019
Deng, He ......................................Poster 254
Deng, Xuchu .................................Poster 295
Denis-Quanquin, Sandrine ..........Poster 298
Denning, Mark ..............................Poster 373
Derochers, Claire .........................Poster 274
Desvaux, Hervé ............................Poster 215
Deveau, Laura ....................... TOD 5:20-5:35
Dey, Krishna .................................Poster 385
Dharan, Nikhil ...............................Poster 157
Dhital, Basant ...............................Poster 078
Didychuk, Allison .........................Poster 043
Diederichs, Jost ...........................Poster 424
Diehl, Anne ...................................Poster 083
Ding, Shangwu .............................Poster 405
Ding, Shangwu .............................Poster 382
Dingemans, Theo J. .....................Poster 376
Dixon, Nicholas ............................Poster 108
Dodd, Stephen..............................Poster 447
Dogan, Fulya ................................Poster 415
Donchev, Alexander .............. TOD 4:50-5:05
Donohue, Matthew .......................Poster 116
Dorn, Harry C. ..............................Poster 245
Dotta, Claudio ...................... ThOD 5:15-5:30
Doty, F. David ...............................Poster 446
Doty, F. David .......................ThOE 5:45-6:00
Doty, Glenn ..........................ThOE 5:45-6:00
Doty, Judy ............................ThOE 5:45-6:00
Downes, Daniel ............................Poster 350
Downing, Keith .............................Poster 078
Dracinsky, Martin .........................Poster 090
Drake, Melanie..............................Poster 259
Draney, Adrian.................. WOB 12:15-12:30
Drobny, Gary ................................Poster 101
D'Souza, Victoria ............... MOB 12:15-12:30
Du, Yi ............................................Poster 408
Duan, Qi .......................................Poster 447
Dubroca, Thierry ..........................Poster 256
Dubroca, Thierry ..........................Poster 255
Dubroca, Thierry ..........................Poster 262
Duer, Melinda ...................... ThOD 4:25-4:50
Duffort, Victor ........................ MOE 5:45-6:30
Dumez, Jean-Nicolas ....................Poster 384
Dumez, Jean-Nicolas ......... TOC 12:00-12:15
Duncan, Roy.................................Poster 033
Dunn, Michael F. ..........................Poster 040
Dunn, Michael F. ................. ThOD 5:30-5:45
Dural, Nezih ..................................Poster 441
Durney, Michael ................ MOB 12:15-12:30
Duss, Olivier ...................... MOB 11:10-11:35
Dutta, Kaushik .......................MOD 5:15-5:30
Dutta, Supratik .................. WOB 11:35-12:00
Duyn, Jeff .....................................Poster 192
Dybowski, Cecil .................... MOE 4:25-4:50
Dzyuba, Sergei .............................Poster 089
Eaton, Hugh .................................Poster 335
Eberly, Lynn .................................Poster 193
Eddy, Matthew ..............................Poster 117
Edison, Arthur ..............................Poster 357
Edison, Arthur ..............................Poster 442
Eghbalnia, Hamid .........................Poster 160
Eichhorn, Tim...............................Poster 251
Eichmann, Cedric .........................Poster 063
Einstein, Samuel ..........................Poster 193
Eliav, Uzi ......................................Poster 173
Program Code: M, T, W, Th, F = Day
O = Oral Time
Eliav, Uzi...................................... Poster 294
Eliezer, David....................... ThOD 5:45-6:00
Elkhaled, Adam ........................... Poster 200
Elliot, K. Wade ............................. Poster 038
Ellis, Paul..................................... Poster 446
Ellis, Paul............................. ThOE 5:45-6:00
Elnatan, Daniel ............................ Poster 068
Elumalai, Malathy ........................ Poster 449
Elyashberg, Mikhail ..................... Poster 155
Emery, Samuel ............................ Poster 157
Emondts, Meike .......................... Poster 267
Emsley, Lyndon .....................MOE 4:50-5:15
Emsley, Lyndon ........................... Poster 108
Emsley, Lyndon ........................... Poster 083
Emsley, Lyndon ........................... Poster 129
Emsley, Lyndon ........................... Poster 263
Emsley, Lyndon ........................... Poster 293
Emsley, Lyndon ........................... Poster 379
Emsley, Lyndon ........................... Poster 414
Emsley, Lyndon ........................... Poster 396
Emsley, Lyndon ........................... Poster 456
Emsley, Lyndon ............... ThOB 11:35-11:50
Emsley, Lyndon ................. TOB 12:00-12:15
Engelke, Frank ............................ Poster 108
Engelke, Frank ............................ Poster 263
Engelke, Frank ............................ Poster 414
Engelke, Frank ............................ Poster 456
Entzminger, George .................... Poster 446
Entzminger, George ............ ThOE 5:45-6:00
Ernst, Matthias............................. Poster 074
Ernst, Matthias............................. Poster 148
Ernst, Matthias................. ThOB 11:10-11:35
Ernst, Matthias..................... ThOD 5:15-5:30
Ertas, Yavuz ................................ Poster 202
Eshuis, Nan ....................... FOB 12:15-12:30
Espinosa, Catalina ...................... Poster 445
Estrada-Reyes, Rosa .................. Poster 327
Evans, Ann M .............................. Poster 303
Fahim, Arjang .............................. Poster 168
Fahmy, Amr F. ............................. Poster 153
Falk, Alexander ............................ Poster 081
Falk, Alexander ............................ Poster 082
Fanucci, Gail ............................... Poster 256
Farndale, Richard ................ ThOD 4:25-4:50
Farrar, Christian ........................... Poster 180
Faucher, Alexandra ..................... Poster 417
Fechler, Nina ............................... Poster 403
Fedorov, Sergey V....................... Poster 144
Feigon, Juli .................................. Poster 041
Feiters, Martin C. ............... FOB 12:15-12:30
Felli, Isabella C. ................ WOB 11:10-11:35
Feng, Yesu .................................. Poster 189
Feng, Zhenhao...................... MOD 4:50-5:15
Fenwick, R. Bryn ......................... Poster 125
Fernandes, Laetitia ...................... Poster 300
Ferrage, Fabien ........................... Poster 130
Ferrage, Fabien ........................... Poster 139
Ferrage, Fabien ........................... Poster 463
Ferrante, Gianni........................... Poster 138
Ferrante, Gianni........................... Poster 457
Ferreira, Fátima ........................... Poster 059
Ferreira, Helen............................. Poster 101
Fey, Michael ................................. Poster 347
Fey, Michael ................................. Poster 346
Fieremans, Els ............................ Poster 218
Figueras, Mercè .......................... Poster 079
Finnigan, James .................. ThOE 4:00-4:25
Firpo, Meri ................................... Poster 193
Fischer, Ran ................................ Poster 250
Fischer, Ran ................................ Poster 249
Fischer, Ran ..................... WOA 09:45-10:00
Poster is followed by board space.
Page 131
INDEX OF AUTHORS
Flores Solis, David....................... Poster 060
Florian, Pierre .............................. Poster 389
Florian, Pierre .............................. Poster 454
Follett, Shelby .............................. Poster 038
Forman, Chris ......................ThOD 4:25-4:50
Forse, Alexander C. ...................... Poster 375
Fortier-McGill, Blythe ................... Poster 347
Fortier-Mcgill, Blythe ................... Poster 346
Fortier-McGill, Blythe ................... Poster 371
Fowler, C. Andrew ........................ Poster 057
Francis, Matt ................................ Poster 121
Franks, Joshua............................. Poster 070
Franks, Trent ................................ Poster 083
Frederick, Kendra ........................ Poster 118
Fredriksson, Jonas ...................... Poster 165
Freedberg, Daron ......................... Poster 048
Freudl, Roland.............................. Poster 103
Freund, Christian .......................... Poster 184
Frey, Merideth .............................. Poster 441
Friščić, Tomislav .......................... Poster 390
Fristrup, Peter .............................. Poster 320
Froehlke, Michael ......................... Poster 466
Frueh, Dominique .............. MOB 11:35-12:00
Frydman, Lucio ..................... MOE 4:00-4:25
Frydman, Lucio ............................ Poster 179
Frydman, Lucio ............................ Poster 249
Frydman, Lucio ............................ Poster 255
Frydman, Lucio ............................ Poster 262
Frydman, Lucio ............................ Poster 250
Frydman, Lucio ................ ThOA 09:20-09:35
Frydman, Lucio .................WOA 09:45-10:00
Fu, Riqiang ................................... Poster 100
Fu, Riqiang ................................... Poster 420
Fugariu, Ioana .............................. Poster 371
Fuglestad, Brian ........................... Poster 035
Fujimoto, Lynn ............................. Poster 031
Fujioka, Koji ................................. Poster 462
Fujiwara, Toshimichi .......... ThOE 4:50 - 5:15
Funkhouser, Gary P. ................... Poster 396
Furihata, Kazuo............................ Poster 321
Furihata, Kazuo............................ Poster 428
Fürtig, Boris.................................. Poster 015
Fyon, Franck ................................ Poster 454
G N, Manjunatha Reddy ................ Poster 285
Gabel, Frank ................................. Poster 022
Gaebel, Torsten ............................ Poster 264
Gagnon, Marie-Claude ................. Poster 071
Gajan, David ................................. Poster 379
Gajan, David ................................. Poster 396
Gajan, David ..................... ThOB 11:35-11:50
Gallagher, Clare N. ...................... Poster 352
Gallagher, Kevin........................... Poster 415
Gambarota, Giulio ........................ Poster 175
Gambarota, Giulio ........................ Poster 201
Gamez, Jeffrey D. ......................... Poster 209
Gan, Zhehong ........................ MOE 4:00-4:25
Gan, Zhehong ............................... Poster 106
Gan, Zhehong ............................... Poster 452
Ganesan, Karthikeyan .................. Poster 263
Gangaplara, Arunakumar ............. Poster 363
Gao, Qi ......................................... Poster 025
Gao, Zhongwei ............................. Poster 030
Garai, Somenath........................... Poster 211
Garon, Ariane ...................ThOC 11:35-12:00
Garrett, Timothy ........................... Poster 357
Garvey, Mark ................................ Poster 315
Garwood, Michael ........................ Poster 187
Garwood, Michael ........................ Poster 193
Garwood, Michael ............ ThOA 08:30-08:55
Gath, Julia ............................ThOD 5:15-5:30
Gayen, Anindita ............................ Poster 098
Gayen, Anindita ............................Poster 126
Ge, Xinmin ....................................Poster 166
Gebregiworgis, Teklab.................Poster 363
Gebregiworgis, Teklab...... TOC 11:10-11:35
Gehrcke, Jan-Philip ......................Poster 011
Geiger, Yasmin ...................TOA 09:20-09:45
Gelenter, Martin............................Poster 395
Gelis, Ioannis ................................Poster 014
Gerald, Rex ..................................Poster 421
Gershoni, David ...........................Poster 249
Gershoni, David ...........................Poster 250
Gershoni, David ............... WOA 09:45-10:00
Ghose, Ranajeet ....................MOD 5:15-5:30
Ghosh, Santanu ...........................Poster 120
Giammatteo, Paul ........................Poster 461
Gierth, Peter .................................Poster 316
Gigmes, Didier..............................Poster 229
Gill, Michelle .................................Poster 152
Gill Jr., Richard.............................Poster 111
Giller, Karin ..................................Poster 017
Giller, Karin ......................... ThOD 4:50-5:15
Ginthör, Stephan ..........................Poster 215
Giorgetti, Sofia ...................TOB 12:00-12:15
Giraud, Nicolas ...................FOB 12:00-12:15
Giraud, Nicolas .............................Poster 298
Giraudeau, Patrick........................Poster 277
Giraudeau, Patrick........................Poster 345
Giraudeau, Patrick............. TOC 12:00-12:15
Gjersing, Erica .............................Poster 089
Gladden, Lynn ..............................Poster 455
Glanzer, Simon ...................FOB 10:45-11:10
Glanzer, Simon .............................Poster 287
Glaser, Niklas J ............... ThOC 11:35-12:00
Glaser, Steffen..............................Poster 170
Glaser, Steffen..............................Poster 283
Glaser, Steffen................. ThOC 11:35-12:00
Glebov, Alexei ..............................Poster 242
Glebov, Leonid .............................Poster 242
Glushka, John ..............................Poster 070
Glushka, John ..............................Poster 444
Gochin, Miriam .............................Poster 341
Gochin, Miriam .............................Poster 342
Goerke, Steffen ............................Poster 186
Goerke, Steffen ............................Poster 196
Goerke, Steffen ............................Poster 176
Goerke, Steffen ................ThOA 09:30-09:50
Goga, Andrei.................................Poster 248
Gogotsi, Yury ...............................Poster 375
Goldbach, Pierre ..........................Poster 016
Goldbourt, Amir ...........................Poster 294
Goldbourt, Amir .................TOA 10:00-10:15
Goldbourt, Amir .................... TOD 5:05-5:20
Golotvin, Sergey ..........................Poster 155
Golotvin, Sergey ..........................Poster 332
Gomes, Muller ..............................Poster 121
Gomes, Muller ..............................Poster 269
Gomes-Neto, Francisco................Poster 141
Gong, Bo ......................................Poster 094
Goobes, Gil ........................TOA 09:20-09:45
Good, Jeremy ...............................Poster 432
Goodrich, Andrew ............. MOB 11:35-12:00
Goodson, Boyd ............................Poster 272
Goodson, Boyd M. .......................Poster 275
Goodson, Boyd M. .......................Poster 273
Goodson, Boyd M. .......................Poster 247
Goodson, Boyd M. .......................Poster 260
Goodson, Boyd M. .......................Poster 243
Goodwin, David............................Poster 164
Gordon, Jeremy ...........................Poster 200
Gordon, Jeremy ...........................Poster 189
Gore, John ....................................Poster 196
Program Code: M, T, W, Th, F = Day
Page 132
O = Oral Time
Gorissen, Antonie........................ Poster 346
Gor'Kov, Peter ............................. Poster 449
Gor'kov, Peter L. ......................... Poster 086
Gor'kov, Peter L. ......................... Poster 452
Gor'kov, Peter L. ......................... Poster 469
Görling, Benjamin........................ Poster 328
Gossert, Alvar.............................. Poster 002
Gotfredsen, Charlotte H. ............. Poster 320
Goto, Atsushi ............................... Poster 454
Goto, Atsushi ....................... ThOE 5:30-5:45
Gouilleux, Boris ................. TOC 12:00-12:15
Govindaraju, Kaushik .................. Poster 195
Gowda, G. A. Nagana .................. Poster 359
Gowda, G. A. Nagana .................. Poster 360
Gowda, Yashas ........................... Poster 359
Gowda, Yashas ........................... Poster 360
Grage, Stephan............................ Poster 076
Graham, Kenneth ........................ Poster 401
Graham, Melanie ......................... Poster 193
Gramigna, Lucia .......................... Poster 285
Grandinetti, Philip ....................... Poster 385
Grau-Campistany, Ariadna ......... Poster 071
Gray, George ............................... Poster 427
Gray, Jeffrey ...................... TOA 09:20-09:45
Gray, John ................................... Poster 225
Graziadei, Andrea........................ Poster 022
Gremer, Lothar ............................ Poster 080
Grewe, Felix................................. Poster 297
Grey, Clare P. .............................. Poster 375
Grey, Clare P. .............................. Poster 414
Grey, Clare P. ................... WOC 12:15-12:30
Grice, Peter ................................. Poster 352
Griesinger, Christian ................... Poster 124
Griesinger, Christian ................... Poster 280
Griffin, John M. ............................ Poster 375
Griffin, Robert .............................. Poster 087
Griffin, Robert .............................. Poster 104
Griffin, Robert .............................. Poster 117
Griffin, Robert .............................. Poster 253
Griffin, Robert .............................. Poster 265
Grishaev, Alexander .................... Poster 127
Griveau, Jean Christophe ............ Poster 406
Gronenborn, Angela.......... TOA 08:30-08:55
Gronenborn, Angela M. ............... Poster 007
Gruning, Wolfram R......... ThOB 11:35-11:50
Grzesiek, Stephan ....................... Poster 150
Gu, Meng ..................................... Poster 191
Gubensäk, Nina................. FOB 10:45-11:10
Gueiros-Filho, Frederico José ..... Poster 061
Guiga, Angelo .............................. Poster 463
Guiga, Angelo ...................... ThOE 5:15-5:30
Gul-E-Noor, Farhana ................... Poster 128
Gul-E-Noor, Farhana ................... Poster 122
Guleria, Anupam .......................... Poster 348
Guma, Monica.............................. Poster 354
Güntert, Peter .............................. Poster 002
Guo, Jerry Jin............................... Poster 307
Guo, Qianni.................................. Poster 240
Guo, Qianni.................................. Poster 308
Gupta, Rupal ..................... TOA 08:30-08:55
Gust, Brogan ............................... Poster 275
Guy, Schoehn .................... MOB 12:00-12:15
Habeck, Michael .................... TOD 4:00-4:25
Habenstein, Birgit .................. TOD 5:05-5:20
Hackenberger, Christian.. ThOA 09:50-10:05
Hagelin-Weaver, Helena ... FOB 11:10-11:35
Hagelin-Weaver, Helena ............. Poster 252
Hagn, Franz ................................. Poster 032
Hagn, Franz ................................. Poster 067
Haider, Ali .................................... Poster 412
Haies, Ibraheem........................... Poster 072
Poster is followed by board space.
INDEX OF AUTHORS
Haies, Ibraheem ........................... Poster 075
Hall, Kathleen ............................... Poster 134
Halouska, Steven ...............TOC 11:10-11:35
Halse, Meghan ............................. Poster 129
Hamaed, Hiyam ..................... MOE 4:00-4:25
Hamilton, Keith .................. TOB 12:15-12:30
Hammann, Blake .......................... Poster 157
Hammann, Blake .......................... Poster 394
Hammer, John A........................... Poster 024
Han, Kee Sung ............................. Poster 416
Han, Oc Hee ................................. Poster 372
Han, Oc Hee ................................. Poster 422
Han, Songi .................................... Poster 464
Han, Song-I................................... Poster 261
Hanna, John ................................. Poster 432
Hansen, D. Flemming ......... FOA 09:45-10:00
Hao, Fuhua ................................... Poster 364
Harden, Bradley ................ MOB 11:35-12:00
Harkema, Susan........................... Poster 205
Harkema, Susan........................... Poster 206
Harper, Jim .......................ThOC 12:00-12:15
Harpole, Kyle................................ Poster 118
Hashi, Kenjiro ............................... Poster 454
Hashi, Kenjiro ....................... ThOE 5:30-5:45
Hashimoto, Yasuhiro ................... Poster 404
Haupt, Erhard T.K......................... Poster 211
Hayamizu, Kikuko......................... Poster 296
Hayamizu, Kikuko......................... Poster 374
Hayden, Mike ............................... Poster 434
Hayes, Sophia .............................. Poster 157
Hayes, Sophia E. .......................... Poster 219
Hayes, Sophia E. .......................... Poster 233
Hayes, Sophia E. .......................... Poster 397
Hayes, Sophia E. .......................... Poster 394
Haynes, Christy ............................ Poster 187
He, Ping ........................................ Poster 223
He, Y............................................. Poster 369
He, Yiyong .................................... Poster 370
Hegemann, Peter ......................... Poster 083
Heil, Werner.................................. Poster 232
Heil, Werner.................................. Poster 230
Heil, Werner...................... WOC 10:45-11:10
Heinmaa, Ivo ................................ Poster 373
Heise, Henrike .............................. Poster 080
Heist, Leah M. .............................. Poster 376
Heitmann, Bjoern ......................... Poster 169
Heitmann, Björn ........................... Poster 315
Hell, Johannes .............................. Poster 045
Hellen, Christopher ............ MOB 12:15-12:30
Helmus, Jonathan ........................ Poster 158
Helmus, Jonathan J...................... Poster 110
Helmy, Adel .................................. Poster 352
Hemmy, Laura .............................. Poster 174
Henriques, Sonia ......................... Poster 076
Henry, Chrystèle ........................... Poster 002
Henry, Geneive E. .............. FOB 11:35-12:00
Herisson, Fanny ..................... TOE 5:05-5:20
Hernández, Gonzalo .................... Poster 169
Herndon, Sierra ............................ Poster 421
Herzfeld, Judith ............................ Poster 087
Hetts, Steven ................................ Poster 465
Hildebrand, Marcel................ MOE 4:00-4:25
Hill, Stephen ................................. Poster 255
Hill, Stephen ................................. Poster 256
Hill, Steve ..................................... Poster 262
Hiller, Sebastian ................. TOB 11:10-11:35
Hirsh, David A. ............................. Poster 387
Hirshman, Nathan ........................ Poster 031
Hoatson, Gina .............................. Poster 136
Hoch, Jeffrey ................................ Poster 158
Hoch, Jeffrey C. .................. FOB 11:35-12:00
Hoeck, Casper ..............................Poster 320
Hoevener, Jan-Bernd ...................Poster 433
Hoff, Daniel ...................................Poster 274
Höfflin, Jens .................................Poster 439
Hoffman, Roy ...............................Poster 427
Holland, Gregory P. ......................Poster 407
Holmes, Sean ........................ MOE 4:25-4:50
Holte, Laura ..................................Poster 446
Holte, Laura ..........................ThOE 5:45-6:00
Hong, Mei .....................................Poster 092
Hong, Mei .....................................Poster 093
Hong, Mei .....................................Poster 095
Hong, Mei .....................................Poster 091
Honorato, Rodrigo Vargas............Poster 061
Hooker, Jerris ...............................Poster 442
Hornak, Joseph ............................Poster 378
Hou, Guangjin .....................TOA 08:30-08:55
Hovey, Liam .................................Poster 057
Howe, Duncan J. ..........................Poster 352
Hoyer, Wolfgang ...........................Poster 080
Hoyt, David W...............................Poster 466
Hsu, Shang-Te Danny ..................Poster 073
Hu, Jian Zhi ...................................Poster 295
Hu, Jian Zhi ...................................Poster 381
Hu, Jian Zhi ...................................Poster 377
Hu, Jian Zhi ...................................Poster 380
Hu, Jun ..................................MOD 5:45-6:00
Hu, Mary .......................................Poster 377
Hu, Mary .......................................Poster 381
Hu, Mary .......................................Poster 380
Hu, Mary Yang ..............................Poster 295
Hu, Yili ..........................................Poster 364
Huang, Chih-Ting..........................Poster 073
Huang, Kuoying ............................Poster 261
Huang, Mitchell .............................Poster 152
Huang, Rui ...................................Poster 058
Huang, Tai-huang .........................Poster 463
Huang, Wenlin ..............................Poster 079
Huang, Wenyu ..............................Poster 270
Huang, Yining ...............................Poster 122
Huber, Gaspard ............................Poster 215
Hugon, Cedric ......................ThOE 5:15-5:30
Hung, Ivan ............................. MOE 4:00-4:25
Hung, Ivan ....................................Poster 106
Hung, Ivan ....................................Poster 086
Hung, Ivan ....................................Poster 469
Hunkeler, Andreas............... ThOD 5:15-5:30
Hurd, Ralph ..................................Poster 191
Hurley, Katie .................................Poster 187
Hurt, Ed ........................................Poster 001
Huster, Daniel...............................Poster 011
Hutchins, Howard.........................Poster 346
Hutchins, Howard.........................Poster 347
Hutchinson, Peter J. ....................Poster 352
Hwang, Dennis .............................Poster 182
Hwang, Dennis .............................Poster 183
Hwang, Dennis .............................Poster 436
Hwang, Ryeo Yun .........................Poster 422
Hyacinthe, Jean-Noel ...................Poster 203
Hyacinthe, Jean-Noël ...................Poster 251
Hyberts, Sven...............................Poster 156
Hyberts, Sven G. ..........................Poster 167
Iddir, Hakim ..................................Poster 415
Idehara, Toshitaka .............. ThOE 4:50 - 5:15
Idso, Matthew ...............................Poster 401
Iguchi, Seiya.........................ThOE 5:30-5:45
Ikura, Mitsu ............................MOD 4:50-5:15
Ikura, Mitsu ...................................Poster 069
Iline-Vul, Taly .....................TOA 09:20-09:45
Illes, Zsolt .....................................Poster 363
Illyés, Tünde Z. .............................Poster 326
Program Code: M, T, W, Th, F = Day
O = Oral Time
Ilott, Andrew ..................... WOC 12:15-12:30
Im, Sang-Choul ............................ Poster 058
Imai, Shunsuke .................. MOB 12:15-12:30
Inoue, Yoshihisa .......................... Poster 404
Iordanescu, George .................... Poster 195
Iqbal, Anwar ................................. Poster 141
Iqbal, Zohaib ................................ Poster 208
Iqbal, Zohaib .......................... TOE 5:35-5:50
Irving, Brian A. ............................. Poster 365
Isas, J Mario ................................ Poster 082
Isern, Nancy ................................ Poster 466
Isley, William ................................ Poster 245
Isoya, Junichi .................... WOA 09:45-10:00
Itin, Boris...................................... Poster 079
Itin, Boris.............................. ThOD 5:45-6:00
Jacquot, Yves.............................. Poster 039
Jagannathan, N. R. ..................... Poster 352
Jähnig, Fabian ................. ThOB 11:10-11:35
Jahnke, Justin.............................. Poster 401
Jahnke, Wolfgang ................. MOD 4:00-4:25
Jalloh, Ibrahim ............................. Poster 352
Janda, Kenneth............................ Poster 307
Jang, Albert ..................... ThOA 08:30-08:55
Jannin, Sami ........................ MOD 5:30-5:45
Jannin, Sami ............................... Poster 236
Jannin, Sami ............................... Poster 362
Jannin, Sami ............................... Poster 384
Jannin, Sami ................... ThOB 11:35-11:50
Janssen, Gerrit ................ ThOB 12:20-12:35
Jaremko, Lukasz ......................... Poster 017
Jaremko, Lukasz ......................... Poster 124
Jaremko, Mariusz ........................ Poster 017
Jaremko, Mariusz ........................ Poster 124
Jaremko, Matt J. .......................... Poster 065
Jarenwattananon, Nanette.......... Poster 202
Jaroniec, Christopher .................. Poster 107
Jaroniec, Christopher P. .............. Poster 110
Jaroniec, Christopher P. .............. Poster 112
Jaroniec, Christopher P. ...... TOA 08:55-9:20
Jaroszewicz, Michael ............MOE 4:00-4:25
Jarvis, James .............................. Poster 072
Jarvis, James .............................. Poster 075
Jayasubba, Reddy....................... Poster 288
Jeerage, Kavita ............................ Poster 027
Jensen, Pernille Rose .................. Poster 271
Jeon, Jaekyun.............................. Poster 096
Jeong, Keunhong ........................ Poster 121
Jeong, Keunhong ........................ Poster 269
Jeong, Keunhong ............. WOA 10:00-10:15
Jerome, Boisbouvier .......... MOB 12:00-12:15
Jerschow, Alexej ......................... Poster 172
Jerschow, Alexej .............. WOC 12:15-12:30
Jeschke, Gunnar ............... MOB 11:10-11:35
Jevtic, Predrag ............................ Poster 038
Jézéquel, Tangi ........................... Poster 345
Jeziorna, agata ............................ Poster 090
Ji, Fangling .................................. Poster 008
Ji, Xiao ......................................... Poster 236
Jiang, Weiping ............................. Poster 240
Jiang, Weiping ............................. Poster 308
Jiang, Xu ..................................... Poster 192
Jiang, Yunjiang ............................ Poster 086
Johnson, Darren W. .................... Poster 394
Johnson, Duane D. ..................... Poster 270
Johnston, Karen....................MOE 4:00-4:25
Jones, Michael............................. Poster 070
Jorge, Christine ........................... Poster 035
Jung, Kwan-Jin ............................ Poster 205
Jung, Kwan-Jin ............................ Poster 207
Jung, Kwan-Jin ............................ Poster 206
Kaderavek, Pavel ........................ Poster 009
Poster is followed by board space.
Page 133
INDEX OF AUTHORS
Kaiser, Robin................................ Poster 213
Kallash, Linda .............................. Poster 079
Kalodimos, Babis ......................... Poster 047
Kalodimos, Charalampos
Babis .......................... MOB 10:45-11:10
Kamihara, Takayuki ..................... Poster 413
Kaminker, Ilia ............................... Poster 261
Kaminker, Ilia ............................... Poster 464
Kamunde-Devonish, Maisha ....... Poster 394
Kanda, Hisao .....................WOA 09:45-10:00
Kandasamy, Balamurugan ........... Poster 412
Kang, Young Kee ......................... Poster 039
Kaoud, Tamer ....................... MOD 5:15-5:30
Kaplan, Mohammed ..................... Poster 077
Karabanov, Alexander.................. Poster 149
Karlsson, Magnus ........................ Poster 271
Karpuk, Sergei ............................. Poster 230
Karpuk, Sergei ................. WOC 10:45-11:10
Kaseman, Derrick ......................... Poster 119
Kasinadhuni, Aditya..................... Poster 449
Kasinath, Vignesh ........................ Poster 118
Kateb, Fatiha ................................ Poster 300
Kaur, Gurneet ............................... Poster 133
Kausik, Ravinath .......................... Poster 217
Kautz, Roger ................................ Poster 468
Kavanaugh, Arthur ....................... Poster 354
Keeler, Eric ................................... Poster 104
Keeler, Eric ................................... Poster 265
Keinan-Adamsky, Keren .... TOA 09:20-09:45
Kentgens, Arno ................ ThOB 12:20-12:35
Keramisanou, Dimitra .................. Poster 014
Kerr, Adam ................................... Poster 200
Kersten, Kortney .......................... Poster 288
Key, Baris .............................. MOE 5:45-6:30
Key, Baris ..................................... Poster 415
Key, Tim ....................................... Poster 033
Keyes, Philip................................. Poster 332
Khade, Rahul................................ Poster 159
Khago, Domarin ........................... Poster 036
Khago, Domarin ........................... Poster 131
Khanra, Nandish........................... Poster 047
Khetrapal, Cl ................................ Poster 348
Kigawa, Takanori.......................... Poster 042
Kim, Cheon Jung ................... MOE 5:45-6:30
Kim, Hai-Young ............................ Poster 336
Kim, Hyun Na ............................... Poster 372
Kim, M. ......................................... Poster 221
Kim, Moonhee .............................. Poster 222
King, Glenn F ............................... Poster 061
King, Jonathan P .......................... Poster 228
King, Jonathan P .......................... Poster 227
King, Jonathan P .......................... Poster 220
King, Jonathan P ...............WOA 10:00-10:15
Kingsley, Carolyn N. .................... Poster 131
Kinnart, Francois .......................... Poster 406
Kiss, Douglas ............................... Poster 361
Kiss, Sebastian ............................ Poster 438
Kiss, Sebastian Z. ........................ Poster 437
Kitchen, Jason ............................. Poster 469
Klages, Jochen............................. Poster 315
Klika, Karel D ............................... Poster 176
Kline, Michael ............................... Poster 278
Klingler, Robert J. ............ ThOC 12:15-12:30
Klippel, Stefan.............................. Poster 184
Klippel, Stefan.................. ThOA 09:50-10:05
Klosin, J ....................................... Poster 369
Knight, Michael .................. TOB 12:00-12:15
Knot, Benno ................................. Poster 108
Knott, Benno ................................ Poster 414
Knott, Benno ................................ Poster 456
Kobayashi, Naoharu ........ ThOA 08:30-08:55
Kobayashi, Takeshi............... MOE 4:00-4:25
Kobayashi, Takeshi......................Poster 270
Kockenberger, Walter ..................Poster 149
Koers, Eline ..................................Poster 244
Köhling, Sebastian .......................Poster 011
Kohn, David ..................................Poster 094
Komarov, Igor ..............................Poster 076
Kong, Fangming ...........................Poster 331
Koos, Martin .................................Poster 330
Koptyug, Igor ...............................Poster 246
Koptyug, Igor ...............................Poster 235
Koretsky, Alan..............................Poster 447
Koroloff, Sophie ...........................Poster 084
Kortz, Ulrich..................................Poster 412
Korver, Anna .................... WOC 11:35-12:00
Korvink, Jan .................................Poster 451
Korvink, Jan .................................Poster 438
Korvink, Jan .................................Poster 433
Korvink, Jan .................................Poster 439
Korvink, Jan G. ............................Poster 437
Korzhnev, Dmitry..........................Poster 021
Koshlap, Karl M. ...........................Poster 185
Kotler, Samuel..............................Poster 034
Koutcher, Jason ...........................Poster 190
Koutcher, Jason ...........................Poster 355
Koutcher, Jason ...........................Poster 356
Kovacs, Helena ............................Poster 015
Kovacs, Helena ............................Poster 316
Kövér, Katalin ...............................Poster 326
Kovtunov, Kirill .............................Poster 235
Kovtunov, Kirill .............................Poster 246
Kozerke, Sebastian .......... ThOB 11:10-11:35
Kozerski, Lech .............................Poster 137
Kozerski, Lech .............................Poster 340
Kozlyuk, Natalia ...........................Poster 037
Kozlyuk, Natalia ...........................Poster 131
Krachmalnicoff, Andrea ...............Poster 373
Krahn, Alex...................................Poster 108
Krahn, Alex...................................Poster 456
Krahn, Alexander ..........................Poster 414
Krajewski, Marcin ............. ThOB 11:10-11:35
Kramer, Gary ................................Poster 427
Kramer, Stephen ..........................Poster 051
Krásný, Libor ................................Poster 020
Kreutz, Cristoph............................Poster 029
Krishnamoorthy, Janarthanan .....Poster 034
Krishnamurthy, Sridevi ................Poster 347
Krishnamurthy, Sridevi ................Poster 346
Krivdin, Leonid .............................Poster 143
Krivdin, Leonid .............................Poster 144
Kroeker, Scott ..............................Poster 104
Kroenke, Christopher ...................Poster 197
Krug, Robert .......................TOB 12:15-12:30
Kryukov, Eugeny ..........................Poster 432
Kuban, Vojtech .............................Poster 044
Kubicki, Dominik J........................Poster 263
Kudla, Ryan ..................................Poster 398
Kuehn, Till ....................................Poster 169
Kuehn, Till ....................................Poster 315
Kuemmerle, R ..............................Poster 369
Kugler, Martin ...............................Poster 424
Kuhns, Philip ................................Poster 258
Kulpanovich, Alex .............. TOA 09:20-09:45
Kumar, Ajeet.................................Poster 352
Kumar, Ashutosh ..........................Poster 120
Kumar, Dinesh..............................Poster 348
Kumar, Pawan ..............................Poster 352
Kumar, Rajeev..............................Poster 346
Kumar, Rajeev..............................Poster 347
Kumar, Virendra ...........................Poster 352
Kumar Vasa, Suresh ........... ThOD 4:50-5:15
Program Code: M, T, W, Th, F = Day
Page 134
O = Oral Time
Kunda, Shailaja ........................... Poster 005
Kunz, Patrick ............................... Poster 176
Künze, Georg............................... Poster 011
Kupce, Eriks ................................ Poster 278
Kupce, Eriks ................................ Poster 316
Kuprov, Ilya ................................. Poster 075
Kuprov, Ilya ................................. Poster 164
Kuprov, Ilya ................................. Poster 146
Kuprov, Ilya ....................... TOC 12:00-12:15
Kurhanewicz, John................ TOE 4:50-5:05
Kurimoto, Tomomitsu .................. Poster 296
Kurita, Jun-ichi............................. Poster 428
Kweon, Jin Jung .......................... Poster 420
Ladbury, John ................... TOB 12:15-12:30
Ladd, Mark E ............................... Poster 186
Ladd, Mark E. .............................. Poster 196
Ladizhansky, Vladimir ................. Poster 086
Ladizhansky, Vladimir ................. Poster 116
Lafon, Olivier ............................... Poster 102
Lai, Jinfeng .................................. Poster 398
Lalli, Daniela ................................ Poster 108
Lalli, Daniela ................................ Poster 456
Lam, Leayen ................................ Poster 346
Lama, Bimala ............................... Poster 350
Lange, Adam ......................... TOD 5:05-5:20
Langen, Ralf ................................ Poster 082
LaPierre, Cristen.......................... Poster 177
LaPierre, Cristen.......................... Poster 429
Lapinaite, Audrone ...................... Poster 022
Laraoui, Abdelghani..................... Poster 431
Larson, Peder .............................. Poster 189
Larson, Peder E. Z. ..................... Poster 200
Lavery, Laura .............................. Poster 068
Lawrence, Chad .......................... Poster 466
Le, Dao ........................................ Poster 229
Le Guennec, Adrien........... TOC 12:00-12:15
Le Marchand, Tanguy ................. Poster 108
Le Marchand, Tanguy ....... TOB 12:00-12:15
Le Ster, Caroline .......................... Poster 201
Leavesley, Alisa .......................... Poster 464
Leblanc, Regan ........................... Poster 029
Lecoq, Lauriane ........................... Poster 026
Ledbetter, Micah P ...................... Poster 220
Lee, Ae-Ree ................................. Poster 046
Lee, Chia-Ying ............................. Poster 183
Lee, D. John................................. Poster 065
Lee, Elizabeth M. Y. ........... TOA 09:20-09:45
Lee, Jaehyuk ................................ Poster 358
Lee, Jae-Seung ............................ Poster 172
Lee, Jae-Seung ...................... TOE 5:20-5:35
Lee, John ..................................... Poster 088
Lee, Joon-Hwa ............................. Poster 046
Lee, Joon-Hwa ............................. Poster 013
Lee, Joon-Hwa ............................. Poster 135
Lee, Jung Ho................................ Poster 127
Lee, Michelle ................................ Poster 093
Lee, Woonghee ............................ Poster 160
Leftin, Avigdor ............................. Poster 190
Leftin, Avigdor ............................. Poster 355
Leftin, Avigdor ............................. Poster 356
Leggett, Jim ..................... ThOB 12:20-12:35
Lehmkuhl, Sören ......................... Poster 266
Lei, Shulei .......................... TOC 11:10-11:35
Leiner, David ................... ThOC 11:35-12:00
Lelli, Moreno ................................ Poster 263
Lelli, Moreno ................................ Poster 379
Leninger, Maureen ...................... Poster 098
Leninger, Maureen ...................... Poster 126
Leonard, Paul .................... TOB 12:15-12:30
Lerche, Mathilde H....................... Poster 271
Lercher, Johannes A. .................. Poster 377
Poster is followed by board space.
INDEX OF AUTHORS
Lesage, Anne ............................... Poster 263
Lesage, Anne ............................... Poster 293
Lesage, Anne ............................... Poster 396
Lesage, Anne ............................... Poster 379
Lesage, Anne ................... ThOB 11:35-11:50
Lesanovsky, Igor ......................... Poster 149
Leung, Hoi Tik Alvin ..................... Poster 150
Levine, Emma H ........................... Poster 220
Levitt, Malcolm ...................TOC 12:00-12:15
Levy, Daniel.................................. Poster 038
Lewandowski, Jozef .................... Poster 129
Lewis, David ................................. Poster 458
Li, Fang ........................................ Poster 127
Li, Haidong ................................... Poster 199
Li, Haidong ................................... Poster 338
Li, Hua .......................................... Poster 196
Li, Ning ......................................... Poster 364
Li, Shi ........................................... Poster 424
Li, Yang ........................................ Poster 056
Li, Yifei.......................................... Poster 152
Li, Yiran ........................................ Poster 228
Li, Yongjun ....................... ThOB 12:05-12:20
Li, Zhao ........................................ Poster 453
Liaghati Mobarhan, Yalda ........... Poster 347
Liang, Hongjun ............................. Poster 086
Liao, Zuolei ................................... Poster 386
Lillaney, Prasheel......................... Poster 465
Lim, Jackwee................................ Poster 118
Lim, Victor ............................ ThOE 4:00-4:25
Lima, Lidia .................................... Poster 343
Lin, Ping-Chang ............................ Poster 140
Linser, Rasmus J. ................ThOD 4:50-5:15
Lipton, Andrew S.......................... Poster 466
Lipton, Stuart A. ........................... Poster 063
Litvak, Ilya .................................... Poster 469
Litvak, Ilya .................................... Poster 452
Liu, Benjamin................................ Poster 309
Liu, Gang-yu ................................. Poster 418
Liu, Jun......................................... Poster 295
Liu, Jun......................................... Poster 416
Liu, Lin.......................................... Poster 030
Liu, Yuanyuan .............................. Poster 171
Live, David ................................... Poster 444
Live, David H. ............................... Poster 070
Lodi, Alessia ................................. Poster 354
Loening, Nikolaus M. ................... Poster 064
Lohans, Christopher T. ................. Poster 053
London, Paz................................. Poster 249
London, Paz................................. Poster 250
London, Paz......................WOA 09:45-10:00
Long, Brandon.............................. Poster 415
Long, Joanna ............................... Poster 256
Long, Joanna ............................... Poster 350
Long, Joanna R. ........................... Poster 262
Long, Joanna R. ............... ThOB 10:45-11:10
Longhini, Andrew ......................... Poster 029
Lopez, Maria................................. Poster 023
Loquet, Antoine ..................... TOD 5:05-5:20
Loria, J. Patrick ............................ Poster 132
Loria, J. Patrick ............................ Poster 161
Lorieau, Justin...................WOB 12:15-12:30
Losey, Aaron ................................ Poster 465
Louis, John M............................... Poster 003
Lu, Manman........................ TOA 08:30-08:55
Lu, Xi ............................................ Poster 431
Lu, Xingyu .......................... TOA 08:30-08:55
Lucena, Guillermo ........................ Poster 367
Luchinat, Claudio ......................... Poster 265
Lucier, Bryan E.G. ........................ Poster 387
Luna, Héctor ................................. Poster 327
Lund, Alicia................................... Poster 464
Luo, Qing ......................................Poster 240
Luo, Qing ......................................Poster 308
Luptak, Andrej ..............................Poster 037
Lustig, Michael .............................Poster 200
Lustig, Michael .............................Poster 189
Lustig, Michael .............................Poster 248
Luy, Burkhard ...............................Poster 283
Luy, Burkhard ...............................Poster 330
Luy, Burkhard ...............................Poster 325
Luy, Burkhard ...............................Poster 319
Luy, Burkhard ...............................Poster 328
Lv, Guohua .......................... ThOD 5:45-6:00
M, Chandrakala .............................Poster 281
Ma, Li-Chung.................................Poster 068
Ma, Li-Chung.......................TOB 12:15-12:30
Ma, Zayd .......................................Poster 219
Ma, Zayd .......................................Poster 394
Ma, Zayd L. ...................................Poster 233
Maas, Werner ...............................Poster 347
Maas, Werner E. ...........................Poster 346
Macek, Pavel ..................... MOB 12:00-12:15
Maciejewski, Mark........................Poster 158
MacKinnon, Neil ...........................Poster 439
Macura, Slobodan.........................Poster 209
Maeda, Hideaki .............................Poster 454
Maeda, Hideaki .....................ThOE 5:30-5:45
Magdoom, Kulam .........................Poster 449
Mager, Dario .................................Poster 438
Mahoney, Brendan ............. TOB 10:45-11:10
Maisano, Federico ........................Poster 271
Majumdar, Ananya .......................Poster 066
Majumder, Subhabrata .................Poster 019
Malik, Nikita ..................................Poster 120
Mall, Shyam S...............................Poster 123
Malon, Michal ...............................Poster 090
Maly, Thorsten ..............................Poster 443
Malz, F ..........................................Poster 369
Mamin, H. J. .................................Poster 221
Mamin, John .................................Poster 222
Mammoli, Daniele..................MOD 5:30-5:45
Mammoli, Daniele.........................Poster 236
Mammoli, Daniele.........................Poster 384
Mance, Deni .................................Poster 244
Mankinen, Otto .............................Poster 231
Manley, Gregory ...........................Poster 161
Mao, Haiyan ..................................Poster 122
Mao, Kanmi ...................................Poster 408
Maolanon, Alex R. ........................Poster 320
Marassi, Francesca ......................Poster 031
Marassi, Francesca ......................Poster 163
Marbella, Lauren ..........................Poster 393
Marbella, Lauren ..........................Poster 391
Marchanka, Alexander .................Poster 022
Marchanka, Alexander ....... TOA 09:45-10:00
Marcio Squina, Fabio ...................Poster 052
Mareci, Thomas ............................Poster 449
Marino, John P. ............................Poster 337
Marjanska, Malgorzata .................Poster 174
Markley, John L. ...........................Poster 043
Markley, John L. ...........................Poster 160
Marquand, Rodrigue.....................Poster 039
Marquardsen, Thorsten ................Poster 139
Marques, Bryan ............................Poster 035
Marquez, Sara ..............................Poster 066
Marsden, Brian .....................ThOE 4:00-4:25
Marsh, Andrew .............................Poster 285
Marshall, Christopher B .........MOD 4:50-5:15
Marshall, Darrell ................ TOC 11:10-11:35
Marshall, Devon ...........................Poster 014
Martel, Laura ......................... MOE 5:15-5:30
Martel, Laura ................................Poster 406
Program Code: M, T, W, Th, F = Day
O = Oral Time
Martelli, Tommaso ....................... Poster 265
Martin, Alastair............................. Poster 465
Martin, Gary................................. Poster 299
Martin, Gary................................. Poster 304
Martin, Michele ............................ Poster 418
Martin, Michele ............................ Poster 461
Martin, Rachel ............................. Poster 307
Martin, Rachel W. ........................ Poster 037
Martin, Rachel W. ........................ Poster 036
Martin, Rachel W. ........................ Poster 131
Martin, Rachel W. ........................ Poster 445
Martineau, Charlotte .................... Poster 419
Martos Riaño, Vera ......... ThOA 09:50-10:05
Mas, Guillaume .................. MOB 12:00-12:15
Masiero, Stefano ......................... Poster 285
Masiewicz, Pawel ........................ Poster 022
Mason, Andrew ............................ Poster 352
Massi, Francesca................... TOD 5:20-5:35
Massilamany, Chandirasegaran .. Poster 363
Matei, Elena ................................. Poster 007
Mathies, Guinevere.......... ThOB 11:50-12:05
Matlahov, Irina ................... TOA 09:20-09:45
Matsuda, Takaaki ........................ Poster 404
Matsuki, Yoh ..................... ThOE 4:50 - 5:15
Matsumoto, Shinji ....................... Poster 454
Matsumoto, Shinji ............... ThOE 5:30-5:45
Matsunaga, Tatsuya .................... Poster 435
Matt, Lucas .................................. Poster 045
Matzger, Adam ............................ Poster 288
Maucourt, Mickaël ....................... Poster 345
Mauhart, Johannes ............ FOB 10:45-11:10
Maul, Andreas ................... WOC 10:45-11:10
Maury, Olivier............................... Poster 298
Mazhab-Jafari, Mohammad .. MOD 4:50-5:15
Mazhab-Jafari, Mohammad T. ..... Poster 069
Mazzola, Eugene ......................... Poster 333
McCallister, Drew ........................ Poster 185
McCallister, Drew ........................ Poster 239
McCallum, Scott .......................... Poster 023
McCarten, J. Riley ....................... Poster 174
McCarthy, Lauren ........................ Poster 258
McCarthy, Michael ....................... Poster 461
McCoy, Mark ............................... Poster 336
McCoy, Mark ............................... Poster 335
McCree, David ..................... ThOE 5:45-6:00
Mccullough, Christopher ............. Poster 366
McDermott, Ann .............. ThOB 12:05-12:20
Mcdermott, Ann................... ThOD 5:45-6:00
McDonald, James ........................ Poster 432
McGehee, Michael ....................... Poster 401
McGill, Stephen ........................... Poster 258
Mckay, Ryan ................................ Poster 053
McNerny, Erin .............................. Poster 094
Medéia De Campos Ramos, B.... Poster 052
Medeiros Oliveira Valença, V ..... Poster 062
Medrano, Brianna ........................ Poster 051
Medronho, Bruno ........................ Poster 297
Mehta, Hardeep ........................... Poster 466
Meier, Beat .................................. Poster 074
Meier, Beat .................................. Poster 148
Meier, Beat .......................... ThOD 5:15-5:30
Meijer, Jan ................................... Poster 216
Meints, Gary A. ............................ Poster 051
Meissner, Jan-Eric ....................... Poster 186
Meissner, Jan-Eric ........... ThOA 09:30-09:50
Meissner, Markus ........................ Poster 438
Meissner, Markus V. .................... Poster 437
Mekap, D ..................................... Poster 369
Melacini, Giuseppe ............ TOB 11:35-12:00
Meldrum, Tyler ............................ Poster 225
Melzi, Roberto .................. ThOB 11:35-11:50
Poster is followed by board space.
Page 135
INDEX OF AUTHORS
Meng, Lu ...................................... Poster 030
Meng Yu, Lucy ............................. Poster 395
Menon, David K. ........................... Poster 352
Meriles, Carlos ............................. Poster 216
Meriles, Carlos ............................. Poster 431
Merlet, Céline ............................... Poster 375
Metz, Gerlinde .............................. Poster 361
Meyer, Helge ................................ Poster 012
Meyer, N.Helge................... FOB 10:45-11:10
Miao, Yimin................................... Poster 100
Michael, Lauren............................ Poster 043
Michaelis, Vladimir K. ................... Poster 104
Michaelis, Vladimir K. ................... Poster 265
Michal, Carl A. .............................. Poster 212
Michel, Erich...................... MOB 11:10-11:35
Miclet, Emeric............................... Poster 039
Miclet, Emeric............................... Poster 362
Miele, Matthew M.......................... Poster 365
Miki, Takashi ................................ Poster 454
Miki, Takashi ........................ ThOE 5:30-5:45
Milani, Jonas ......................... MOD 5:30-5:45
Milani, Jonas ................................ Poster 236
Milani, Jonas ................................ Poster 362
Milani, Jonas ................................ Poster 384
Milani, Jonas .................... ThOB 11:35-11:50
Milikisiyants, Sergey ................... Poster 116
Miller, Luke A D ............................ Poster 303
Miller, M ....................................... Poster 369
Miller, Mark................................... Poster 057
Millstone, Jill ................................ Poster 391
Millstone, Jill ................................ Poster 393
Millward, Niki................................ Poster 358
Milon, Alain................................... Poster 103
Milshteyn, Eugene ................. TOE 4:50-5:05
Miragoli, Luigi............................... Poster 271
Mirecka, Ewa................................ Poster 080
Mishra, Prasanna K. ..................... Poster 209
Mishra, Subrata ................. MOB 11:35-12:00
Miskolzie, Mark ............................ Poster 053
Misra, Durga ................................. Poster 348
Misra, R N .................................... Poster 348
Mittermaier, Anthony K ...... FOA 08:30-08:55
Miyamoto, Tetsuo ........................ Poster 454
Miyamoto, Tetsuo ................ ThOE 5:30-5:45
Mizuno, Takashi ........................... Poster 462
Mizuno, Takashi ........................... Poster 435
Mizushima, Ryota ........................ Poster 004
Mogami, Yuuki ............................. Poster 462
Mohammadi, Mohaddese. WOC 12:15-12:30
Moing, Annick............................... Poster 345
Mokhun, Oleksiy........................... Poster 242
Molinas, Marisa ............................ Poster 079
Mollica, Giulia............................... Poster 268
Monaco, Stephen ......................... Poster 398
Mondal, Somnath ......................... Poster 339
Monette, Martine .......................... Poster 346
Monette, Martine .......................... Poster 347
Montelione, Gaetano ................... Poster 068
Montelione, Gaetano ......... TOB 12:15-12:30
Montelione, Gaetano ............ TOD 4:25-4:50
Montina, Tony .............................. Poster 361
Montina, Tony .............................. Poster 459
Montina, Tony .............................. Poster 458
Moore, Eric ................................... Poster 460
Moore, Jeremy ............................. Poster 157
Moore, Jeremy K. ......................... Poster 397
Moorman, Veronica ...................... Poster 118
Moraes, Adolfo ............................. Poster 059
Moraes, Adolfo ............................. Poster 141
Morag, Omry ...................... TOA 10:00-10:15
Morag, Omry ......................... TOD 5:05-5:20
Moremen, Kelley ..........................Poster 025
Moremen, Kelley W. .....................Poster 030
Morgan, Brittany .................... TOD 5:20-5:35
Morgan, Steven W. .......................Poster 224
Moriaud, Fabrice ..........................Poster 169
Moriscot, Christine ............ MOB 12:00-12:15
Morris, Gareth A. ..........................Poster 326
Morris, Laura ................................Poster 068
Morris, Michael .............................Poster 094
Morrison, Emma .............. WOB 11:35-12:00
Morze, Cornelius ...........................Poster 189
Moscato, Beth ..............................Poster 132
Mottillo, Cristina ...........................Poster 390
Mroue, Kamal ...............................Poster 094
Mroue, Kamal ...............................Poster 288
Mueller, Karl .................................Poster 416
Mueller, Karl .................................Poster 466
Mueller, Leonard ..........................Poster 398
Mueller, Leonard J. .......................Poster 040
Mueller, Leonard J. .............. ThOD 5:30-5:45
Mukherjee, Sujoy .........................Poster 123
Mukhopadhyay, Dwaipayan .........Poster 107
Müller, Achim................................Poster 211
Müller, Henrik ...............................Poster 080
Müller, Norbert..............................Poster 214
Müller, Norbert..............................Poster 215
Münnemann, Kerstin ....................Poster 232
Muñoz, Lisa ..................................Poster 064
Munro, Rachel ..............................Poster 116
Munson, Eric ................................Poster 310
Munson, Eric ................................Poster 448
Murakami, Kimiya .........................Poster 404
Murakami, Miwa ...........................Poster 413
Murata, Yasujiro ...........................Poster 373
Murphy, Anna ........................ MOE 4:25-4:50
Murphy, Michael P........................Poster 352
Murphy-Boesch, Joseph ..............Poster 447
Mykhailiuk, Pavel .........................Poster 076
N, Lokesh ......................................Poster 286
N, Lokesh ......................................Poster 276
Nadaud, Philippe S. ......................Poster 110
Nadaud, Philippe S. ..............TOA 08:55-9:20
Nadav-Tsubery, Merav....... TOA 09:20-09:45
Nagarajarao, Suryaprakash..........Poster 276
Nagarajarao, Suryaprakash..........Poster 286
Nakamatsu, Keith .........................Poster 049
Nakamura, Shinji ................ThOE 4:50 - 5:15
Nakamura, Tomohiro ....................Poster 063
Namespetra, Andrew............. MOE 4:00-4:25
Nasr, Mahmoud ............................Poster 032
Nast, Robert E. .............................Poster 442
Nath, Nilamoni ..............................Poster 280
Navon, Gil.....................................Poster 173
Nazar, Linda .......................... MOE 5:45-6:30
Ndukwe, Ikenna............................Poster 284
Neal, Luke...........................FOB 11:10-11:35
Nelson, Amanda ...........................Poster 323
Nemoto, Takahiro .........................Poster 454
Nemoto, Takahiro .................ThOE 5:30-5:45
Nethercott, Matthew .....................Poster 310
Nethercott, Matthew .....................Poster 448
Neto Moreira Ferreira, Dinarte .....Poster 062
Nevzorov, Alexander A. ................Poster 084
Nevzorov, Alexander A. ................Poster 147
Nevzorov, Alexander A. ................Poster 446
Newman, Timothy .........................Poster 418
Ni, Qing Zhe..................................Poster 087
Nichols, Scott .................... MOB 11:35-12:00
Nie, Guangjun ...............................Poster 364
Niederländer, Benjamin................Poster 232
Nielsen, Helle ...............................Poster 363
Program Code: M, T, W, Th, F = Day
Page 136
O = Oral Time
Nielsen, Niels Chr. ........... ThOC 11:10-11:35
Niemöller, Arvid ........................... Poster 464
Nieuwkoop, Andrew .................... Poster 083
Nikiel, Anna ...................... WOC 10:45-11:10
Nikolaou, Panayiotis (Peter) ........ Poster 272
Nikoloau, Panayiotis .................... Poster 275
Nilsson, Mathias .......................... Poster 326
Nirma, Charlotte........................... Poster 343
Niroomand, Shahriar ................... Poster 336
Nishijima, Gen............................. Poster 454
Nishijima, Gen..................... ThOE 5:30-5:45
Nishikawa, Tadateru.................... Poster 069
Nishiyama, Yusuke...................... Poster 094
Nishiyama, Yusuke...................... Poster 085
Nishiyama, Yusuke...................... Poster 288
Nishiyama, Yusuke...................... Poster 454
Nishyama, yusuke ....................... Poster 090
Noeske, Ralph ............................. Poster 191
Noguchi, Takashi ................ ThOE 5:30-5:45
Noguchi, Takeshi ........................ Poster 454
Nogueira, Maria Luiza Caldas...... Poster 061
Novikov, Dmitry S. ....................... Poster 218
Nucci, Nathaniel .......................... Poster 035
Nyarko, Afua................................ Poster 001
Nyman, May ................................ Poster 386
O'Brien, Evan .............................. Poster 035
O'brien, Paul................................ Poster 142
O'Donnell, Lauren F. ................... Poster 311
Ogumi, Zempachi ........................ Poster 413
Ohki, Shinobu .............................. Poster 454
Ohki, Shinobu ...................... ThOE 5:30-5:45
Ohliger, Michael .......................... Poster 189
Ohno, K. ...................................... Poster 221
Ohno, Kenichi .............................. Poster 222
Okamura, Hideyasu ..................... Poster 042
O'keefe, Christopher .................... Poster 390
Okuno, Yusuke ............................ Poster 257
Oliveira, Paulo Sergio Lopes ....... Poster 061
Olsen, Christian A. ....................... Poster 320
Omichinski, James G. ................. Poster 026
Ong, Ta-Chung ............................ Poster 104
Ong, Ta-Chung ............................ Poster 265
Onoda, Shinobu ................ WOA 09:45-10:00
Opella, Stanley ............................ Poster 113
Opella, Stanley ............................ Poster 105
Opella, Stanley ............................ Poster 115
Opella, Stanley ............................ Poster 163
Opyr, Michael............................... Poster 458
Opyr, Michael............................... Poster 459
Orts, Julien ........................... MOD 4:25-4:50
Oschkinat, Hartmut ..................... Poster 083
Osen, David ................................. Poster 108
Osen, David ................................. Poster 414
Osen, David ................................. Poster 456
Otten, Ernst Wilhelm ......... WOC 10:45-11:10
Ouari, Olivier................................ Poster 229
Ouari, Olivier................................ Poster 244
Ouari, Olivier................................ Poster 263
Ouari, Olivier................................ Poster 379
Owers-Bradley, John .................. Poster 214
Paciok, Eva ................................. Poster 266
Page, Ralph ...................... WOA 10:00-10:15
Palmer, Arthur G .......................... Poster 142
Palmer, Melissa ................. FOB 11:35-12:00
Palmer, Melissa ........................... Poster 154
Paluch, Piotr ................................ Poster 102
Paluch, Piotr ................................ Poster 090
Pan, Huilin.................................... Poster 416
Pandey, Manoj ............................. Poster 085
Pandey, Manoj ............................. Poster 094
Pandey, Manoj ............................. Poster 288
Poster is followed by board space.
INDEX OF AUTHORS
Pandey, Manoj Kumar .................. Poster 454
Papaioannou, Antonios ................ Poster 128
Papaioannou, Antonios ................ Poster 218
Papas, Klearchos.......................... Poster 193
Paquin, Jean-Francois.................. Poster 071
Parella, Teodor ...................TOC 12:15-12:30
Park, Sang Ho .............................. Poster 115
Park, Sang Ho .............................. Poster 105
Parker, Anna ................................ Poster 228
Parker, Anna ................................ Poster 467
Pashley, Clare L. .......................... Poster 117
Patriarchi, Tommaso.................... Poster 045
Patwardhan, Neeraj ..................... Poster 323
Paul, Schanda ................... MOB 12:00-12:15
Pawlak, Tomasz ........................... Poster 090
Peat, David ................................... Poster 214
Pecharsky, Vitalij K. ..................... Poster 270
Peden, Charles H. F. .................... Poster 377
Peden, Charles H.F. ..................... Poster 381
Pederson, Kari ............................. Poster 068
Pelczer, Istvan .............................. Poster 309
Pell, Andrew J............................... Poster 414
Pelupessy, Philippe...................... Poster 009
Pelupessy, Philippe...................... Poster 130
Peng, Jeffrey ...................... TOB 10:45-11:10
Penzel, Susanne........................... Poster 104
Pérez, Herminia ............................ Poster 327
Perras, Frederic ............................ Poster 270
Pestova, Tatyana .............. MOB 12:15-12:30
Peterkofsky, Alan..............WOB 12:00-12:15
Peters, Gretchen Marie................. Poster 285
Petina, Olga A. ............................. Poster 211
Pezzagna, Sebastien .................... Poster 216
Pham, Wellington.......................... Poster 247
Phan, Chanh V. ............................ Poster 079
Phan, Trang .................................. Poster 229
Phillipps, David ............................ Poster 432
Piana, Stefano ....................... TOD 4:50-5:05
Pickard, John D. ........................... Poster 352
Piechalska, Barbara ..................... Poster 232
Piechatzek, Timo.......................... Poster 080
Pines, Alex ................................... Poster 121
Pines, Alex ................................... Poster 228
Pines, Alex ................................... Poster 227
Pines, Alex ................................... Poster 269
Pines, Alex ................................... Poster 455
Pines, Alex ........................WOA 10:00-10:15
Pines, Alexander .......................... Poster 220
Pines, Alexander .......................... Poster 226
Pinon, Arthur ................................ Poster 293
Pintacuda, Guido ......................... Poster 083
Pintacuda, Guido ......................... Poster 108
Pintacuda, Guido ......................... Poster 414
Pintacuda, Guido ......................... Poster 456
Pintacuda, Guido ............... TOB 12:00-12:15
Pirko, Istvan ................................. Poster 209
Pisabarro, Mayte .......................... Poster 011
Piserchio, Andrea ................. MOD 5:15-5:30
Plückthun, Andreas ..................... Poster 067
Pol, Rostislav ................................ Poster 332
Polenova, Tatyana ............. FOB 11:35-12:00
Polenova, Tatyana ....................... Poster 090
Polenova, Tatyana ............. TOA 08:30-08:55
Poppe, Leszek.............................. Poster 334
Porter, Elizabeth........................... Poster 273
Pöschko, Maria Theresia ............. Poster 214
Pöschko, Maria Theresia ............. Poster 215
Potrzebowski, Marek ................... Poster 090
Potrzebowski, Marek ................... Poster 102
Powers, Robert ............................ Poster 363
Powers, Robert ..................TOC 11:10-11:35
Pozhidaeva, Alexandra.................Poster 021
Pradhan, Dev Ranjan ...................Poster 312
Presser, Volker .............................Poster 375
Prestegard, James .......................Poster 068
Prestegard, James .......................Poster 025
Prestegard, James .......................Poster 070
Prestegard, James H. ..................Poster 030
Prestegard, James H. ..................Poster 444
Prigent, Yann ...............................Poster 327
Proctor, Aaron ..............................Poster 051
Proffit, Danielle...................... MOE 5:45-6:30
Prudden, Anthony.........................Poster 030
Pruski, Marek ........................ MOE 4:00-4:25
Pruski, Marek ...............................Poster 270
Pulido, Sergio-Andres ..................Poster 012
Purdy, Andrew ..............................Poster 400
Purea, Armin .................................Poster 108
Purea, Armin .................................Poster 263
Purea, Armin .................................Poster 414
Purea, Armin .................................Poster 456
Qi, Zhe ..........................................Poster 112
Qi, Zhe ..................................TOA 08:55-9:20
Qian, Chunqi .................................Poster 447
Qiu, S ...........................................Poster 369
Qiu, Xiaohua .................................Poster 279
Quessette, Franck ........................Poster 419
Quinn, Caitlin ......................TOA 08:30-08:55
Raatz, Nicole.................................Poster 216
Rabanal, Francesc........................Poster 071
Rabatinová, Alžběta .....................Poster 020
Radbruch, Alexander ...................Poster 186
Radbruch, Alexander ....... ThOA 09:30-09:50
Rademann, Jörg ...........................Poster 011
Radford, Sheena ..........................Poster 117
Radoicic, Jasmina ........................Poster 115
Raftery, Daniel ..............................Poster 360
Raftery, Daniel ..............................Poster 359
Raghothama, S. ...........................Poster 018
Rainey, Jan ..................................Poster 033
Raiola, Luca .................................Poster 026
Rajan, Rakesh ..................... ThOD 4:25-4:50
Raleigh, Daniel .............................Poster 054
Ramakrishnan, Venkatesh ....MOD 5:15-5:30
Ramamoorthy, Ayyalusamy .........Poster 034
Ramamoorthy, Ayyalusamy .........Poster 058
Ramamoorthy, Ayyalusamy .........Poster 094
Ramamoorthy, Ayyalusamy .........Poster 085
Ramamoorthy, Ayyalusamy .........Poster 288
Ramamurthi, Kumaran .................Poster 111
Ramaswamy, Vijaykumar .............Poster 442
Ranta, Kaili ...................................Poster 275
Raschle, Thomas .........................Poster 032
Ravera, Enrico ..............................Poster 265
Ravikovitch, Peter........................Poster 408
Ravula, Thirupathi.........................Poster 339
Rawat, Atul ...................................Poster 348
Rayner, Grant ...............................Poster 424
Read, Jolene .................................Poster 033
Reardon, Patrick N .......................Poster 466
Reat, Valerie .................................Poster 103
Reddy, Jay ...................................Poster 363
Redwine, D...................................Poster 369
Reed, Galen..................................Poster 200
Reed, Galen............................TOE 4:50-5:05
Regatte, Ravinder .........................Poster 172
Regatte, Ravinder ...................TOE 5:20-5:35
Reibarkh, Mikhail ..........................Poster 299
Reichert, Johannes ......................Poster 071
Reichhardt, Courtney ...................Poster 109
Reichhardt, Courtney ...................Poster 099
Reid, David G ...................... ThOD 4:25-4:50
Program Code: M, T, W, Th, F = Day
O = Oral Time
Reif, Bernd ................................... Poster 073
Reif, Bernd ........................... ThOD 4:00-4:25
Reilly, David ................................ Poster 264
Reilly, David ................................ Poster 234
Reimer, Jeffrey ............................ Poster 259
Reimer, Jeffrey ............................ Poster 395
Reimer, Jeffrey ................. WOC 11:10-11:35
Reinhard, Friedemann ................. Poster 216
Reinke, Stefan ................. ThOA 09:50-10:05
Reinsperger, Tony....................... Poster 283
Rej, Ewa....................................... Poster 264
Reller, Malin................................. Poster 324
Ren, Lili ........................................ Poster 338
Renault, Marie ............................. Poster 103
Reno, John .................................. Poster 258
Renslow, Ryan ............................ Poster 466
Repetto, Maricel .......................... Poster 232
Repetto, Maricel .......................... Poster 230
Rerich, Eugenia ........................... Poster 186
Rerich, Eugenia ........................... Poster 188
Rettner, C. T. ............................... Poster 221
Rettner, Charles .......................... Poster 222
Reverdatto, Sergey ..................... Poster 019
Reyes, Arneil ............................... Poster 258
Reynolds, Chris ........................... Poster 051
Reynolds, William F..................... Poster 306
Ribeiro, Anthony A....................... Poster 303
Ricagno, Stefano ............... TOB 12:00-12:15
Rice, David .................................. Poster 097
Rice, David .................................. Poster 099
Rice, David M............................... Poster 109
Richter, Christian ......................... Poster 015
Ridge, Clark D. ............................ Poster 311
Ridge, Clark D. ............................ Poster 333
Riedo, Elisa ................................. Poster 431
Riek, Roland ......................... MOD 4:25-4:50
Riek, Roland ................................ Poster 006
Riek, Roland ................................ Poster 049
Riek, Roland ................................ Poster 063
Ring, Hattie .................................. Poster 187
Riobé, François............................ Poster 298
Ritcey, Anna M. ........................... Poster 387
Rivillas-Acevedo, Lina ................ Poster 010
Roberts, Lawrence R. .................. Poster 396
Robinson, Anne ............... WOB 11:35-12:00
Robson, Scott .............................. Poster 156
Robson, Scott .............................. Poster 167
Robustelli, Paul ..................... TOD 4:50-5:05
Roche, Julien ............................... Poster 003
Rodin, Victor ................................ Poster 215
Rodrigues, Flávio Aparecido ....... Poster 399
Rogawski, Rivkah............ ThOB 12:05-12:20
Rogawski, Rivkah................ ThOD 5:45-6:00
Rokem, Ariel ................................ Poster 191
Romalis, Michael ......................... Poster 441
Romaniuk, Joe Anthony .............. Poster 109
Romaniuk, Joseph....................... Poster 097
Rorick, Amber.............................. Poster 159
Rose, Honor................................. Poster 184
Rose, Honor..................... ThOA 09:50-10:05
Rosen, Matthew ........................... Poster 181
Rosen, Matthew ........................... Poster 178
Rosen, Matthew ........................... Poster 180
Rosen, Matthew ........................... Poster 177
Rosen, Matthew ........................... Poster 234
Rosen, Matthew ........................... Poster 275
Rosen, Matthew ........................... Poster 272
Rosen, Matthew ........................... Poster 247
Rosen, Matthew ........................... Poster 429
Rosen, Matthew ........................... Poster 450
Rosen, Matthew ........................... Poster 430
Poster is followed by board space.
Page 137
INDEX OF AUTHORS
Rosen, Matthew ..................... TOE 5:05-5:20
Ross, Alfred .................................. Poster 016
Rossella, Federica ....................... Poster 184
Rossi, Paolo ................................. Poster 047
Rossini, Aaron ............................. Poster 293
Rossini, Aaron J. .......................... Poster 263
Rossini, Aaron J. .......................... Poster 379
Rossini, Aaron J. .......................... Poster 402
Rossini, Aaron J. .......................... Poster 396
Rouger, Laetitia ..................TOC 12:00-12:15
Roussel, Christophe ..................... Poster 203
Roussel, Christophe ..................... Poster 251
Rout, Ashok .................................. Poster 024
Rovedo, Philipp ............................ Poster 433
Rovny, Jared ................................ Poster 161
Rovnyak, David .................. FOB 11:35-12:00
Rovnyak, David ............................ Poster 154
Rovnyak, David ............................ Poster 365
Rovnyak, James................. FOB 11:35-12:00
Rovó, Petra ..........................ThOD 4:50-5:15
Royappa, Grace ........................... Poster 049
Ruan, Ke ...................................... Poster 008
Ruan, Weiwei ............................... Poster 198
Ruan, Weiwei ............................... Poster 254
Rudd, Michael .............................. Poster 336
Rugar, D. ...................................... Poster 221
Rugar, Daniel ............................... Poster 222
Rupaimoole, Rajesha................... Poster 358
Rusakov, Yury Yu. ....................... Poster 143
Rusakov, Yury Yu. ....................... Poster 144
Rusakova, Irina L. ........................ Poster 143
Russell, John ............................... Poster 415
Rutjes, Floris P.J.T. ............ FOB 12:15-12:30
Ryan, Herbert ............................... Poster 443
Ryan, William................................ Poster 378
Ryasnyanskiy, Aleksandr ............ Poster 242
Ryoo, Ryong................................. Poster 402
S, Marie-Paule .............................. Poster 024
Sachleben, Joseph....................... Poster 151
Sadet, Aude .................................. Poster 300
Sadet, Aude .................................. Poster 362
Saha, Dipta ................................... Poster 258
Saint-Jalmes, Hervé .................... Poster 201
Saint-Jalmes, Hervé .................... Poster 175
Saito, Kazuyoshi ........................... Poster 454
Saito, Kazuyoshi ................... ThOE 5:30-5:45
Sakellariou, Dimitrios ................... Poster 130
Sakellariou, Dimitrios ................... Poster 463
Sakellariou, Dimitrios ........... ThOE 5:15-5:30
Sakuma, Chiseko ......................... Poster 321
Sakuma, Chiseko ......................... Poster 428
Salameh, Najat ............................. Poster 180
Salameh, Najat ............................. Poster 177
Salameh, Najat ............................. Poster 430
Salameh, Najat ....................... TOE 5:05-5:20
Salido, Sandra I. ........................... Poster 245
Salnikov, Oleg.............................. Poster 246
Salnikov, Oleg.............................. Poster 235
Salvati, Roberto............................ Poster 175
Samulski, Edward T. .................... Poster 376
Samultsev, Dmitry O. ................... Poster 144
Šanderová, Hana ......................... Poster 020
Sanders, Gary .............................. Poster 258
Sanders, Kevin ............................. Poster 414
Sanders, Kevin J. ......................... Poster 456
Sandre, Anthony .................... MOE 4:00-4:25
Sangodkar, Rahul P. .................... Poster 396
Santos, Webster ........................... Poster 323
Santos De Freitas, Mônica........... Poster 062
Sarell, Claire J. ............................. Poster 117
Sarker, Muzaddid ......................... Poster 033
Sarracanie, Mathieu .....................Poster 178
Sarracanie, Mathieu .....................Poster 181
Sarracanie, Mathieu .....................Poster 180
Sarracanie, Mathieu .....................Poster 177
Sarracanie, Mathieu .....................Poster 234
Sarracanie, Mathieu .....................Poster 429
Sarracanie, Mathieu .....................Poster 430
Sarracanie, Mathieu .....................Poster 450
Sarracanie, Mathieu ...............TOE 5:05-5:20
Sasaki, Akiko ................................Poster 388
Saurí, Josep .................................Poster 291
Saurí, Josep .................................Poster 290
Saurí, Josep .................................Poster 289
Sauvee, Claire ..............................Poster 244
Sauvée, Claire ..............................Poster 263
Schaefer, Jacob ...........................Poster 317
Schanda, Paul ....................FOA 09:20-09:45
Schatschneider, Bohdan .............Poster 398
Scheler, Ulrich ..............................Poster 383
Schilling, Franz ............................Poster 283
Schlagnitweit, Judith....................Poster 215
Schlagnitweit, Judith....................Poster 293
Schleker, P. Philipp M. .................Poster 267
Schleker, Peter.............................Poster 266
Schmidt, Christian ........................Poster 124
Schmidt, Claudia ..........................Poster 297
Schmidt, Elena .............................Poster 002
Schmidt, Manuel ..........................Poster 280
Schmidt, Rita....................ThOA 09:20-09:35
Schmidt-Rohr, Klaus....................Poster 091
Schnieders, Robbin......................Poster 015
Schrank, Evelyne .........................Poster 012
Schröder, Leif...............................Poster 184
Schröder, Leif...................ThOA 09:50-10:05
Schuenke, Patrick ........................Poster 188
Schuenke, Patrick ........................Poster 194
Schulze Sünninghausen, David ..Poster 325
Schumann, Frank .........................Poster 316
Schurko, Robert ...........................Poster 390
Schurko, Robert W. ............... MOE 4:00-4:25
Schurko, Robert W. ......................Poster 387
Schuyler, Adam ............................Poster 158
Schwalbe, Harald .........................Poster 015
Schwalbe, Harald ............. WOB 10:45-11:10
Schwartz, Julian ...........................Poster 226
Schwarzwalder, Martin..... ThOB 11:35-11:50
Schwarzwälder, Martin.................Poster 263
Schwendeman, Anna ...................Poster 058
Schwieters, Charles .....................Poster 112
Schwieters, Charles .....................Poster 163
Schwieters, Charles .............. TOD 5:35-5:50
Scott, Eric .....................................Poster 259
Scott, Faith ...................................Poster 274
Sears, Jesse .................................Poster 466
Sefler, Andrea M...........................Poster 303
Seginer, Amir....................ThOA 09:20-09:35
Seki, Shiro ....................................Poster 374
Selfslag, Chris ....................... MOE 5:15-5:30
Selfslag, Chris ..............................Poster 406
Seltzer, Scott ................................Poster 226
Semenov, Valentin A. ...................Poster 144
Sen, Sabyasachi ...........................Poster 119
Sengupta, Suvrajit ........................Poster 131
Sengupta, Suvrajit ........................Poster 307
Senguttuvan, Premkumar ..... MOE 5:45-6:30
Seo, Yongbeom ............................Poster 402
Sergeyev, Ivan .................ThOB 12:05-12:20
Sergeyev, Ivan .................... ThOD 5:45-6:00
Serra, Olga ...................................Poster 079
Service, Rachel ............................Poster 081
Service, Rachel ............................Poster 082
Program Code: M, T, W, Th, F = Day
Page 138
O = Oral Time
Sesti, Erika .................................. Poster 219
Sesti, Erika L................................ Poster 233
Sethi, Manish ............................... Poster 310
Settipalle, Neesha ....................... Poster 206
Sforça, Mauricio........................... Poster 052
Sforça, Mauricio Luis ................... Poster 061
Sgourakis, Nikolaos .......... TOA 10:00-10:15
Sgourakis, Nikolaos .............. TOD 5:05-5:20
Shanaiah, Narasimhamurthy ....... Poster 323
Shang, Hong................................ Poster 200
Shang, Hong.......................... TOE 4:50-5:05
Shao, Qi ....................................... Poster 187
Sharma, Manvendra ........ ThOB 12:20-12:35
Sharp, Kim ................................... Poster 118
Shaw, David........................... TOD 4:50-5:05
Shchepin, Roman........................ Poster 243
Shchepin, Roman........................ Poster 247
Shchepin, Roman........................ Poster 260
Shchepin, Roman........................ Poster 273
Shea, Madeline ............................ Poster 057
Shekhtman, Alexander ................ Poster 019
Shemesh, Noam .......................... Poster 179
Shemesh, Noam .............. ThOA 09:20-09:35
Sherwood, M. H. ......................... Poster 221
Sherwood, Mark .......................... Poster 222
Shi, Cheng-Yu.............................. Poster 405
Shi, Fan ....................................... Poster 260
Shi, Fan ....................................... Poster 243
Shi, Fan ....................................... Poster 273
Shi, Hui ........................................ Poster 377
Shi, Yunyu ................................... Poster 008
Shim, Myungbo ............................ Poster 050
Shimabukuro, Jody ..................... Poster 049
Shimizu, Tadashi ......................... Poster 462
Shimizu, Tadashi ......................... Poster 454
Shimizu, Tadashi ................. ThOE 5:30-5:45
Shin, Chang ................................. Poster 226
Shin, Chang ...................... WOA 10:00-10:15
Shin, Peter ................................... Poster 189
Shin, Peter ................................... Poster 248
Shin, Peter ............................. TOE 4:50-5:05
Siaw, Ting Ann ............................. Poster 464
Siemer, Ansgar ............................ Poster 081
Siemer, Ansgar B......................... Poster 082
Silva de Miranda, Mariane .......... Poster 399
Silvers, Robert ............................. Poster 117
Simoes, Rui ................................. Poster 355
Simon, Bernd ............................... Poster 022
Simon, Bernd ..................... TOA 09:45-10:00
Simon, Patrice ............................. Poster 375
Simpson, Andre........................... Poster 347
Simpson, Andre J ........................ Poster 346
Simpson, Andre J ........................ Poster 371
Simpson, Myrna J........................ Poster 346
Singh, Chandan ........................... Poster 128
Singh, Kawarpal .......................... Poster 282
Singh, Khushpreet ....................... Poster 352
Sinha, Anil K. ............................... Poster 182
Sinha, Neeraj ............................... Poster 128
Sirigiri, Jagadishwar .................... Poster 274
Sirigiri, Jagadishwar .......... ThOE 4:50 - 5:15
Sitkowski, Jerzy .......................... Poster 137
Sitkowski, Jerzy .......................... Poster 340
Sjolander, Tobias ........................ Poster 227
Sjolander, Tobias ........................ Poster 455
Sjolander, Tobias F ..................... Poster 220
Slack, Clancy ............................... Poster 121
Slack, Clancy ............................... Poster 269
Slebodnick, Carla........................ Poster 323
Slowing, Igor I. ............................ Poster 270
Smirnov, Alex I. ........................... Poster 116
Poster is followed by board space.
INDEX OF AUTHORS
Smirnov, Alex I. ............................ Poster 446
Smirnov, Vadim ........................... Poster 242
Smirnova, Tatyana ....................... Poster 116
Smith, Adam................................. Poster 256
Smith, Ashley ............................... Poster 391
Smith, Matthew J ................... MOD 4:50-5:15
Smrecki, Vilko .............................. Poster 215
Smrt, Sean ........................WOB 12:15-12:30
Snell, Emily.........................TOC 11:10-11:35
Sohn, Sung-Min ................ ThOA 08:30-08:55
Soleilhavoup, Anne ............. ThOE 5:15-5:30
Solís, Aida .................................... Poster 327
Somers, Joseph .................... MOE 5:15-5:30
Song, Yipeng ................................ Poster 364
Song, Yi-Qiao ............................... Poster 217
Song, Yi-Qiao ............................... Poster 282
Sood, Anil ..................................... Poster 358
Soong, Ronald ............................. Poster 347
Soong, Ronald ............................. Poster 346
Soong, Ronald ............................. Poster 371
Spagna, Stefano ........................... Poster 424
Spencer, Richard.......................... Poster 204
Spengler, Nils............................... Poster 438
Spengler, Nils............................... Poster 451
Spengler, Nils............................... Poster 439
Spengler, Nils............................... Poster 437
Spengler, Nils............................... Poster 440
Spielman, Daniel .......................... Poster 191
Spitzmesser, JB ................... ThOE 5:45-6:00
Srinivasan, Kartik ......................... Poster 023
Staab, John .................................. Poster 446
Staab, John .......................... ThOE 5:45-6:00
Stahlfeld, Philip ............................ Poster 154
Stanek, Jan .................................. Poster 108
Stanek, Jan .................................. Poster 456
Stanley, Ann Marie ............WOB 12:00-12:15
Stanton, Christopher .................... Poster 258
Stark, Jaime ................................. Poster 160
Stark, Ruth E. ............................... Poster 079
Stathopulos, Peter B.................... Poster 069
Staudacher, Tobias ...................... Poster 216
Staveness, Daryl .......................... Poster 317
Steele, Joshua .............................. Poster 329
Stenzoski, Natalie ........................ Poster 054
Stephenson, Shawn ..................... Poster 275
Stern, Raivo.................................. Poster 373
Stetz, Matthew .............................. Poster 035
Stevens, J.C. ................................ Poster 369
Stockmann, Jason ....................... Poster 450
Stöppler, Daniel ........................... Poster 083
Stork, Conrad ............................... Poster 211
Strandberg, Erik ........................... Poster 071
Straney, Patrick ............................ Poster 393
Strickland, Corey ......................... Poster 336
Strickland, Madeleine .......WOB 12:00-12:15
Stronks, Henry ............................. Poster 347
Stronks, Henry J. ......................... Poster 346
Strotz, Dean .......................... MOD 4:25-4:50
Strotz, Dean ................................. Poster 006
Struppe, Jochem .......................... Poster 346
Struppe, Jochem .......................... Poster 347
Struppe, Jochem .......................... Poster 456
Struppe, Jochem .......................... Poster 458
Stteffen, David ............................. Poster 363
Studer, Sonja ............................... Poster 032
Studholme, Colin ......................... Poster 197
Stupp, Gregory ............................. Poster 357
Su, Yongchao ............................... Poster 117
Suematsu, Hiroto ......................... Poster 454
Suematsu, Hiroto ................. ThOE 5:30-5:45
Suematsu, Hiroto ................. ThOE 5:45-6:00
Suiter, Christopher.............. FOB 11:35-12:00
Suiter, Christopher.............. TOA 08:30-08:55
Sun, Shangjin ...............................Poster 152
Sun, Xianping ...............................Poster 199
Sun, Xianping ...............................Poster 198
Sun, Xianping ...............................Poster 254
Sun, Xianping ...............................Poster 453
Sun, Ziqi .......................................Poster 245
Surewicz, Krystyna .......................Poster 110
Surewicz, Krystyna ...............TOA 08:55-9:20
Surewicz, Witold...........................Poster 110
Surewicz, Witold K. ..............TOA 08:55-9:20
Surface, J. Andrew .......................Poster 397
Suszynski, Thomas ......................Poster 193
Suter, Dieter .................................Poster 213
Sutrisno, Andre ............................Poster 371
Swager, Timothy...........................Poster 253
Swapna, G.V.T. ..................TOB 12:15-12:30
Sweeney, Shannon.......................Poster 354
Switala, Lauren.............................Poster 378
Sykora, Stanislav..........................Poster 162
Szilágyi, László ............................Poster 326
Taber, Bob ............................ThOE 4:00-4:25
Takahashi, Masato .......................Poster 454
Takahashi, Masato ...............ThOE 5:30-5:45
Takeda, Kazuyuki .........................Poster 074
Takegoshi, K. ...............................Poster 435
Takegoshi, K. ...............................Poster 462
Takegoshi, Kiyonori......................Poster 413
Tan, Kong Ooi ...............................Poster 148
Tanaka, Ryoji ................................Poster 454
Tanaka, Ryoji ........................ThOE 5:30-5:45
Tang, Huiru ...................................Poster 364
Tang, Huiru ........................ TOC 11:35-12:00
Tashiro, Mitsuru ...........................Poster 321
Tashiro, Mitsuru ...........................Poster 428
Tata, Gopinath ..............................Poster 088
Tatematsu, Yoshinori ......... ThOE 4:50 - 5:15
Tatolo, Godiraone .........................Poster 284
Taulelle, Francis ...........................Poster 419
Tavakoli Dinani, Reza ..................Poster 434
Tayler, Michael .............................Poster 227
Tayler, Michael .............................Poster 455
Tayler, Michael .................ThOB 12:20-12:35
Tedoldi, Fabio ..............................Poster 271
Tefft, Kristin ..................................Poster 057
Telkki, Ville-Veikko .......................Poster 231
Terbrock, Amy..............................Poster 051
Terpstra, Melissa..........................Poster 174
Terrien, Anaïs ...............................Poster 039
Terry, Jeremy ...............................Poster 424
Terskikh, Victor V. ........................Poster 417
Terskikh, Victor V. ........................Poster 394
Tesch, Deanna .............................Poster 084
Tesch, Michael ................ ThOC 11:35-12:00
Tessari, Marco....................FOB 12:15-12:30
Testud, Frederik ...........................Poster 440
Theint, Theint ...............................Poster 110
Theint, Theint .......................TOA 08:55-9:20
Theis, Thomas ..............................Poster 243
Theis, Thomas ..............................Poster 301
Thieuleux, Chloé .............. ThOB 11:35-11:50
Thomas, M. Albert ........................Poster 208
Thomas, M. Albert ..................TOE 5:35-5:50
Thrasher, Daniel ............... WOC 11:35-12:00
Thurber, Kent ...............................Poster 114
Thurber, Kent ................... WOA 09:20-09:45
Thureau, Pierre ............................Poster 268
Thureau, Pierre ............................Poster 229
Tian, Fang ....................................Poster 111
Tian, Ye ........................................Poster 163
Program Code: M, T, W, Th, F = Day
O = Oral Time
Timári, István ............................... Poster 326
Tinoco, Luzineide ........................ Poster 343
Tishmack, Patrick ........................ Poster 427
Tiziani, Stefano ............................ Poster 354
Tjandra, Nico ............................... Poster 024
Tjandra, Nico .................... WOB 12:00-12:15
Toda, Mitsuru ............................... Poster 462
Tokarski III, John ......................... Poster 258
Tokunaga, Yo .............................. Poster 406
Tolman, Joel R ............................ Poster 066
Tonelli, Marco .............................. Poster 043
Tonelli, Marco .............................. Poster 160
Tordo, Paul .................................. Poster 263
Tordo, Paul .................................. Poster 244
Tordo, Paul .................................. Poster 229
Tordo, Paul .................................. Poster 379
Tošner, Zdeněk ............... ThOC 11:10-11:35
Traaseth, Nate ............................. Poster 098
Traaseth, Nate ............................. Poster 126
Trautwein, Christoph ................... Poster 351
Trease, Nicole M. .............. WOC 12:15-12:30
Trebosc, Julien ............................ Poster 102
Trébosc, Julien ............................ Poster 090
Trociewitz, Bianca ....................... Poster 262
Trociewitz, Bianca ....................... Poster 255
Tropis, Marielle ............................ Poster 103
Tropp, James............................... Poster 189
Tropp, James............................... Poster 210
Truong, Milton ............................. Poster 243
Truong, Milton ............................. Poster 247
Truong, Milton ............................. Poster 260
Truong, Milton ............................. Poster 246
Truong, Milton ............................. Poster 273
Truxal, Ashley .............................. Poster 121
Truxal, Ashley .............................. Poster 269
Tullney, Kathlynne ....................... Poster 230
Tycko, Robert .............................. Poster 114
Tycko, Robert .............................. Poster 136
Tycko, Robert .............................. Poster 460
Tycko, Robert ................... WOA 09:20-09:45
Tyndall, Erin ................................ Poster 111
Tzitzilonis, Christos ..................... Poster 063
Uchimoto, Yoshiharu ................... Poster 413
Ulrich, Anne................................. Poster 076
Ulrich, Anne S. ............................ Poster 071
Ulrich, Eldon ................................ Poster 160
Valafar, Homayoun ...................... Poster 168
Valente, Ana Paula ...................... Poster 059
Valente, Ana Paula ...................... Poster 141
Valentine, Kathleen ..................... Poster 035
Valentine, Kathleen ..................... Poster 118
van Belkum, Marco J................... Poster 053
Van Bentum, Jan......................... Poster 443
Van Bentum, Jan............. ThOB 12:20-12:35
Van der Cruijsen, Elwin............... Poster 244
van der Sluis, Eli ......................... Poster 073
van Gelderen, Peter .................... Poster 192
van Kalkerendd, Henri A. ThOB 11:35-11:50
van Meerten, Bas ............ ThOB 12:20-12:35
van Tol, Hans .............................. Poster 262
van Tol, Johan ............................. Poster 255
van Weerdenburg, Bram J. A.FOB 12:15-12:30
Varga, Krisztina............................ Poster 038
Varga, Krisztina............................ Poster 089
Vasa, Suresh Kumar .............. TOD 5:05-5:20
Vasos, Paul Romeo ..................... Poster 300
Vassiliou, Christophoros.............. Poster 121
Vassiliou, Christophoros.............. Poster 269
Vassiliou, Christophoros... WOA 10:00-10:15
Vaughan, Thomas ........... ThOA 08:30-08:55
Vaughey, John.......................MOE 5:45-6:30
Poster is followed by board space.
Page 139
INDEX OF AUTHORS
Vederas, John C. .......................... Poster 053
Veeraperumal, Suresh ................. Poster 355
Veglia, Gianluigi ................. FOA 08:55-09:20
Veglia, Gianluigi ........................... Poster 088
Veinberg, Stanislav ............... MOE 4:00-4:25
Velan, S. Sendhil .................... TOE 4:00-4:25
Venkatasubramanian,
Palamadai ............................. Poster 195
Verma, Deepak............................. Poster 182
Veyre, Laurent .................. ThOB 11:35-11:50
Vial, Sandrine ............................... Poster 419
Viel, Stéphane .............................. Poster 229
Viel, Stéphane .............................. Poster 268
Vigili, Albert ........................TOC 12:15-12:30
Vigneron, Daniel .......................... Poster 189
Vigneron, Daniel .......................... Poster 200
Vigneron, Daniel .......................... Poster 248
Vigneron, Daniel .................... TOE 4:50-5:05
Vijayakumar, M. ........................... Poster 416
Villadsen, Jesper S. ..................... Poster 320
Villinger, Saskia ........................... Poster 124
Vivekanandan, Subramanian ....... Poster 034
Vjunov, Aleksei ............................ Poster 377
Voegeli, Beat ......................... MOD 4:25-4:50
Vogeli, Beat .................................. Poster 006
Vogeli, Beat .................................. Poster 125
von Morze, Cornelius ............. TOE 4:50-5:05
Vora, Ankit .................................... Poster 411
Voreck, Anja ................................. Poster 083
Vosegaard, Thomas ......... ThOC 11:10-11:35
Vostrikov, Vitaly ........................... Poster 088
Vugmeyster, Liliya ....................... Poster 136
Vuichoud, Basile ................... MOD 5:30-5:45
Vuichoud, Basile .......................... Poster 236
Vuichoud, Basile .......................... Poster 384
Vuichoud, Basile .............. ThOB 11:35-11:50
Waddell, Kevin ............................. Poster 246
Waddell, Kevin ............................. Poster 247
Waddington, David ...................... Poster 180
Waddington, David ...................... Poster 177
Waddington, David ...................... Poster 234
Waddington, David ...................... Poster 264
Waddington, David ...................... Poster 429
Waddington, David ...................... Poster 430
Waddington, David ................ TOE 5:05-5:20
Wadhwani, Parvesh ..................... Poster 071
Wagner, Gabriel ........................... Poster 012
Wagner, Gerhard ............... MOB 12:15-12:30
Wagner, Gerhard .......................... Poster 032
Wagner, Gerhard .......................... Poster 055
Wagner, Gerhard .......................... Poster 067
Wagner, Gerhard .......................... Poster 156
Wagner, Gerhard .......................... Poster 153
Wagner, Gerhard .......................... Poster 167
Wald, Lawrence ............................ Poster 450
Wald, Lawrence L. ............ ThOA 08:55-09:20
Walder, Brennan........................... Poster 385
Wales, David ........................ThOD 4:25-4:50
Walish, Joseph ............................. Poster 253
Walker, Thad .................... WOC 11:35-12:00
Wallner, Michael ........................... Poster 059
Wallrabe, Ulrike ............................ Poster 451
Wallrabe, Ulrike ............................ Poster 440
Walls, Jamie ................................. Poster 223
Walls, Jamie D. ............................ Poster 311
Walsworth, Ronald....................... Poster 234
Walter, Eric ................................... Poster 466
Wälti, Marielle ........................ MOD 4:25-4:50
Walz, Thomas ............................... Poster 032
Wand, A. Joshua .......................... Poster 035
Wand, Joshua............................... Poster 118
Wang, Bing ...................................Poster 357
Wang, Bo ......................................Poster 354
Wang, Guangshun ............ WOB 12:00-12:15
Wang, Haijing ...............................Poster 228
Wang, Haijing ................... WOA 10:00-10:15
Wang, Hai-Jing .............................Poster 226
Wang, Hao............................. MOE 5:45-6:30
Wang, Hao....................................Poster 375
Wang, Hong..................................Poster 344
Wang, Hsin ............................MOD 5:15-5:30
Wang, Lei .....................................Poster 049
Wang, Mingzhang ............... TOA 08:30-08:55
Wang, Shenlin ..............................Poster 086
Wang, Shenlin ..............................Poster 116
Wang, Shuo ..................................Poster 025
Wang, Tuo ....................................Poster 092
Wang, Tuo ....................................Poster 091
Wang, Wei ....................................Poster 122
Wang, Wei ....................................Poster 295
Wang, Weimin ..............................Poster 171
Wang, Xiaojie................................Poster 197
Wang, Xiaoling..............................Poster 245
Wang, Xingsheng ............... TOB 10:45-11:10
Wang, Yanfei ................................Poster 238
Wang, Yaqiang .............................Poster 041
Wang, Yulan .................................Poster 364
Wapler, Matthias C .......................Poster 440
Ward, Meaghan ............................Poster 086
Waring, Alan .................................Poster 093
Warner, Lisa .................................Poster 089
Warren, Warren ............................Poster 301
Warren, Warren S. ........................Poster 243
Washton, Nancy ...........................Poster 466
Waskell, Lucy ...............................Poster 058
Wasylishen, Roderick E. ..............Poster 417
Webb, Robert................................Poster 313
Weber, Julia M. .............................Poster 002
Weegman, Bradley .......................Poster 193
Wegner, Sebastian .......................Poster 108
Wegner, Sebastian .......................Poster 414
Wegner, Sebastian .......................Poster 456
Wei, Daxiu ....................................Poster 170
Wei, Xiaoliang ...............................Poster 295
Wei, Xuan .....................................Poster 133
Wei, Xuan .....................................Poster 224
Weimin, Wang ..............................Poster 425
Weingarth, Daniel.........................Poster 375
Weingarth, Markus .......................Poster 244
Weirich, Franziska ........................Poster 080
Wemmer, David ............................Poster 121
Wemmer, David ............................Poster 269
Wender, Paul ................................Poster 317
Wenrich, Broc R. ..........................Poster 365
Wentz, Katherine ..........................Poster 394
Werbeck, Nicolas ............... FOA 09:45-10:00
Werner-Zwanziger, Ulrike ............Poster 400
Wessling, Matthias .......................Poster 266
Westler, William ............................Poster 160
Wheeler, Patrick ...........................Poster 155
Wheeler, Patrick ...........................Poster 332
While, Peter ..................................Poster 438
Whitby, Richard ............................Poster 373
Wi, Sungsool .................................Poster 255
Wi, Sungsool .................................Poster 262
Widdifield, Cory ...........................Poster 293
Widegren, Jason ..........................Poster 302
Widgeon, Scarlett .........................Poster 399
Wiese, Martin ................................Poster 266
Wijmenga, Sybren S........... FOB 12:15-12:30
Wildman, Katherine .......... WOB 11:35-12:00
Willhite, Andrea ............................Poster 206
Program Code: M, T, W, Th, F = Day
Page 140
O = Oral Time
Williams, Jonathan ...................... Poster 091
Williams, Jonathan ...................... Poster 095
Williamson, Philip........................ Poster 072
Williamson, Philip T.F. ................ Poster 075
Williamson, R. Thomas ............... Poster 299
Williamson, Thomas.................... Poster 304
Willmering, Matthew.................... Poster 219
Willmering, Matthew M. ............... Poster 233
Wilson, Neil ........................... TOE 5:35-5:50
Wimperis, Stephen ...................... Poster 388
Windschuh, Johannes ................. Poster 188
Windschuh, Johannes ..... ThOA 09:30-09:50
Winniford, B ................................ Poster 369
Winquist, Nickolas ....................... Poster 310
Winter, Calvin .............................. Poster 459
Wishart, David ................... TOC 10:45-11:10
Wisniewski, Daniel ...................... Poster 149
Withers, Richard .......................... Poster 442
Witherspoon, Velencia ................ Poster 395
Witte, Christopher ........................ Poster 184
Witte, Christopher ............ ThOA 09:50-10:05
Wittmann, Johannes.................... Poster 074
Witzel, Thomas ............................ Poster 177
Woelk, Klaus ................................ Poster 421
Woelk, Klaus .................... ThOC 12:15-12:30
Wojtecki, Rudy ............................ Poster 411
Wong, Gerard .............................. Poster 093
Wong, Veronica ................... ThOD 4:25-4:50
Wood, Ryan ................................. Poster 258
Wood, Travis ............................... Poster 242
Wooler, Bradley ........................... Poster 408
Worley, Bradley ................. TOC 11:10-11:35
Wrachtrup, Joerg ........................ Poster 216
Wren, John .................................. Poster 104
Wu, Bing ...................................... Poster 241
Wu, Chao .......................... WOB 11:35-12:00
Wu, Chin H................................... Poster 105
Wu, Jihui ...................................... Poster 008
Wu, Zhen ..................................... Poster 382
Wyche, Thomas ........................... Poster 299
Wyrwicz, Alice ............................. Poster 195
Wyss, Daniel ................................ Poster 336
Xia, Ding ...................................... Poster 172
Xia, Ding ................................ TOE 5:20-5:35
Xia, Junchao ...................... TOB 10:45-11:10
Xiang, Sheng Qi................... ThOD 4:50-5:15
Xiao, Jie ....................................... Poster 416
Xiaoyun, Zhu ............................... Poster 425
Xie, Junshuai ............................... Poster 453
Xu, Jun......................................... Poster 122
Xu, Jun......................................... Poster 392
Xu, Junzhong ............................... Poster 196
Xu, Qiuwei.................................... Poster 305
Xu, Suochang .............................. Poster 377
Xu, Suochang .............................. Poster 381
Xu, Suochang .............................. Poster 380
Xue, Jing ...................................... Poster 019
Yabe, Atsuko................................ Poster 296
Yamamoto, Kazutoshi ................. Poster 034
Yamazaki, Satoru ........................ Poster 404
Yan, Zhimin .................................. Poster 410
Yanagisawa, Yoshinori ................ Poster 454
Yanagisawa, Yoshinori ........ ThOE 5:30-5:45
Yang, Chen .................................. Poster 398
Yang, Chen .......................... ThOD 5:30-5:45
Yang, Hao .................................... Poster 317
Yang, Liu...................................... Poster 159
Yang, Shengjun ........................... Poster 308
Yang, Xiaodong ........................... Poster 170
Yang, Yu ...................................... Poster 093
Yao, Hongwei ............................... Poster 093
Poster is followed by board space.
INDEX OF AUTHORS
Yao, Yao ................................ MOE 4:25-4:50
Yao, Yefeng .................................. Poster 368
Yao, Yong ..................................... Poster 031
Yarger, Jeffery L ........................... Poster 407
Yates, Jonathan............................ Poster 386
Yau, Wai-Ming .............................. Poster 114
Yau, Wai-Ming ...................WOA 09:20-09:45
Ye, Chaohui .................................. Poster 199
Ye, Chaohui .................................. Poster 198
Ye, Chaohui .................................. Poster 254
Ye, Chaohui .................................. Poster 453
Yesinowski, James ...................... Poster 400
Ying, Jinfa .................................... Poster 127
Youle, Richard .............................. Poster 031
Young, Robert P. .......................... Poster 040
Yu, Liping...................................... Poster 057
Yu, Liping...................................... Poster 349
Yuan, Yaping ................................ Poster 453
Yuan, Yue..................................... Poster 005
Yulikov, Maxim .................. MOB 11:10-11:35
Zacharias, Niki ............................. Poster 366
Zachrdla, Milan ............................ Poster 020
Zagdoun, Alexandre ..................... Poster 379
Zaiss, Moritz ................................. Poster 186
Zaiss, Moritz ................................. Poster 196
Zaiss, Moritz ................................. Poster 188
Zaiss, Moritz ................................. Poster 176
Zaiss, Moritz ................................. Poster 194
Zaiss, Moritz ..................... ThOA 09:30-09:50
Zaitsev, Maxim ............................. Poster 440
Zajicek, Jaroslav........................... Poster 005
Zambrello, Matthew ..................... Poster 158
Zangger, Klaus ................... FOB 10:45-11:10
Zangger, Klaus ............................. Poster 012
Zangger, Klaus ............................. Poster 287
Zeier, Robert.....................ThOC 11:35-12:00
Zeng, Qingbin ...............................Poster 240
Zeng, Qingbin ...............................Poster 308
Zens, Toby............................ThOE 4:00-4:25
Zeri, Ana Carolina de Mattos.........Poster 061
Zerweck, Jonathan .......................Poster 071
Zhang, Bo .......................... TOC 11:10-11:35
Zhang, Huilan .....................TOA 08:30-08:55
Zhang, Huiliang ............................Poster 234
Zhang, Huiting ..............................Poster 453
Zhang, Jiahai ................................Poster 008
Zhang, Jinjin .................................Poster 187
Zhang, Le .....................................Poster 185
Zhang, Le .....................................Poster 239
Zhang, Meng ................................Poster 058
Zhang, Ming .................................Poster 418
Zhang, Rongchun .........................Poster 085
Zhang, Xiaoliang ...........................Poster 465
Zhang, Yong .................................Poster 159
Zhang, Yonghong .........................Poster 045
Zhang, Yuning ..............................Poster 237
Zhang, Zhiying ..............................Poster 199
Zhang, Zhiying ..............................Poster 338
Zhang, Zhiyong.................ThOA 09:20-09:35
Zhang, Ziming...............................Poster 014
Zhao, Evan .........................FOB 11:10-11:35
Zhao, Evan ...................................Poster 252
Zhao, Mitchell ...............................Poster 115
Zhao, Ruifang ...............................Poster 364
Zhao, Xiuchao...............................Poster 199
Zhao, Xiuchao...............................Poster 453
Zhao, Zhenchao............................Poster 380
Zhao, Zhenchao............................Poster 381
Zhao, Zhenchao............................Poster 377
Zheng, Haibin .....................FOB 11:10-11:35
Zheng, Haibin ...............................Poster 252
Zheng, Le .....................................Poster 069
Program Code: M, T, W, Th, F = Day
O = Oral Time
Zhivonitko, Vladimir .................... Poster 231
Zhong, Jianping ........................... Poster 198
Zhong, Jianping ........................... Poster 254
Zhou, Ronghui ................... FOB 11:10-11:35
Zhou, Ronghui ............................. Poster 252
Zhou, Xin ..................................... Poster 199
Zhou, Xin ..................................... Poster 198
Zhou, Xin ..................................... Poster 254
Zhou, Xin ..................................... Poster 240
Zhou, Xin ..................................... Poster 308
Zhou, Xin ..................................... Poster 338
Zhou, Xin ..................................... Poster 453
Zhou, Zhe .................................... Poster 369
Zhou, Zijian .................................. Poster 301
Zhu, Bo ........................................ Poster 180
Zhu, Lingyan ................................ Poster 398
Zhu, Peizhi ................................... Poster 409
Zhu, Zihan.................................... Poster 248
Zhu, Zihan.............................. TOE 4:50-5:05
Zia, Wasif ..................................... Poster 467
Ziarek, Joshua ............................. Poster 067
Ziarelli, Fabio............................... Poster 229
Ziarelli, Fabio............................... Poster 268
Žídek, Lukáš ................................ Poster 020
Zimay, Greg ................................. Poster 260
Zimmer, Stefan ............................ Poster 230
Zintsmaster, John S. ......... TOB 10:45-11:10
Zong, Chengli .............................. Poster 025
Zou, Qin ....................................... Poster 070
Zuiderweg, Erik ........................... Poster 145
Zumbulyadis, Nicholas ..........MOE 4:25-4:50
Zumbulyadis, Nicholas ................ Poster 378
Zuo, Xiaobing ..................... MOB 12:15-12:30
Zussblatt, Niels ........................... Poster 403
Zweckstetter, Markus .................. Poster 017
Zweckstetter, Markus .................. Poster 124
Poster is followed by board space.
Page 141
DIRECTORY OF PARTICIPANTS (as of March 31, 2015)
Sachiko Abe
Taiyo Nippon Sanso Corporation
Tokyo Japan
James Aramini
CABM Rutgers University
Piscataway NJ
Sean Barrett
Yale University Physics Dept.
New Haven CT
Bennett Addison
UC Davis
Davis CA
Luke Arbogast
NIST-IBBR
Rockville MD
Marcos Battistel
Food and Drug Administration
Silver Spring MD
Mobae Afeworki
EMRE
Annandale NJ
Haribabu Arthanari
Harvard Medical School
Boston MA
Thomas Bauer
ETH Zurich
Zurich Switzerland
Hee-Chul Ahn
Deptof Pharmacy, Dongguk University
Goyang Korea
Katsuo Asakura
JEOL Ltd.
Tokyo Japan
Daniel Bernhard Baumann
Bruker-Biospin AG
Faellanden Switzerland
Adewale Akinfaderin
Florida State University
Tallahassee FL
Matthew Augustine
UC Davis
Davis CA
Marvin Bayro
National Institutes of Health
Bethesda MD
Todd M. Alam
Sandia National Laboratories
Albuquerque NM
Claudia Avalos
UC Berkeley
Berkeley CA
Dan Bearden
NIST
Charleston SC
Lawrence B. Alemany
Rice University
Houston TX
Charles Babu
Novartis
Cambridge MA
Owen Becette
University of Maryland
Hyattsville MD
Charlie Alexander
Triangle Analytical, Inc.
Morrisville NC
David Badger
Ashland Inc.
Dublin OH
Johanna Becker
KIT
Eggenstein-Leopoldshafen Germany
Fabio Almeida
Fed. Univ. Rio de Janeiro
Rio de Janeiro Brazil
Vlad Badilita
University of Freiburg
Freiburg im Breisgau Germany
Elzbieta Bednarek
National Medicines Institute
Warsaw Poland
Jesse Alonzo
Quantum Design
San Diego CA
Laima Baltusis
Stanford University
Stanford CA
Alain Belguise
Bruker BioSpin
Wissembourg Cedex France
Gonzalo Agustin Alvarez
Weizmann Institute of Science
Rehovot Israel
James Banigan
New York University
New York NY
George M Benedikt
Lubrizol Advanced Materials
Brecksville OH
Carlos Amero
UAEM
Cuernavaca Mexico
Diego Baptista
Harvard Medical School
Boston MA
Marina Bennati
MPI for Biophysical Chemistry
Göttingen Germany
Samrat Amin
Arizona State University / MRRC
Phoenix AZ
Dan Barabino
JEOL USA
Peabody MA
Tim Bergeron
JEOL USA, INC
Peabody MA
Gisele Amorim
Federal University of Rio de Janeiro
Rio de Janeiro Brazil
Thomas M Barbara
OHSU
Portland OR
Sabrina Berkamp
UCSD
La Jolla CA
Jean Paul Amoureux
Lille University and ECNU Shanghai
Villeneuve d'Ascq France
Emeline Barbet-Massin
Technical Universität München
Garching Germany
Zachariah Berkson
UCSB
Santa Barbara CA
Takahiro Anai
JEOL Resonance
Tokyo Japan
Michael J. Barlow
University of Nottingham
Nottingham UK
Guillermo Bermejo
National Institutes of Health
Bethesda MD
Clemens Anklin
Bruker BioSpin
Billerica MA
Alexander Barnes
Washington University in St. Louis
St. Louis MO
Wolfgang Bermel
Bruker BioSpin
Rheinstetten Germany
Drake Anthony
Southern Illinois University - Carbondale
Carbondale IL
Christopher Barr
University of Victoria
Victoria BC Canada
Bob Berno
McMaster University
Hamilton ON Canada
Sachiko.Abe@tn-sanso.co.jp
jbaddison@ucdavis.edu
mobae.afeworki@exxonmobil.com
hcahn@dongguk.edu
aaa12g@my.fsu.edu
tmalam@sandia.gov
lalemany@rice.edu
charlie@triangleanalytical.com
fabioceneviva@gmail.com
jesse@qdusa.com
gonzalo.a.alvarez@weizmann.ac.il
carlosamero@uaem.mx
samrat.amin@gmail.com
giseleamorim@me.com
jean-paul.amoureux@univ-lille1.fr
anai@jeol.co.jp
clemens.anklin@bruker.com
styropyro@siu.edu
Page 142
jma@cabm.rutgers.edu
arbogastl@ibbr.umd.edu
hari@hms.harvard.edu
katsuo.asakura@j-resonance.com
maugust@ucdavis.edu
cavalos3@gmail.com
charles.babu@novartis.com
dbbadger@ashland.com
vlad.badilita@imtek.de
laimab@stanford.edu
banigan@nyu.edu
baptista@fas.harvard.edu
dbarabino@jeol.com
barbarat@ohsu.edu
ebarbetm.ens@gmail.com
michael.barlow@nottingham.ac.uk
barnesab@wustl.edu
cbarr@uvic.ca
sean.barrett@yale.edu
marcos.battistel@fda.hhs.gov
toba@nmr.phys.chem.ethz.ch
daniel.baumann@bruker.com
marvin.bayro@nih.gov
dan.bearden@nist.gov
obecette@umd.edu
johanna.becker@kit.edu
e.bednarek@nil.gov.pl
alain.belguise@bruker.com
george.benedikt@lubrizol.com
mbennat@gwdg.de
tbergeron@jeol.com
saberkam@ucsd.edu
zberkson@umail.ucsb.edu
bermejog@mail.nih.gov
wolfgang.bermel@bruker.com
bberno@mcmaster.ca
DIRECTORY OF PARTICIPANTS (as of March 31, 2015)
Pierrick Berruyer
ENS Lyon
Villeurbanne France
Mustapha Bouhrara
National Institute on Aging, NIH
Baltimore MD
Estel Canet
EPFL
Lausanne Switzerland
Jan Bierma
UC, Irvine
Irvine CA
Richard Bounds
University of Southampton
Southampton UK
Andrea Capozzi
IPSB - EPFL
Lausanne Switzerland
Terri Bishop
SP Scientific
Stone Ridge NY
Clifford R Bowers
Chemistry Dept, University of Florida
Gainesville FL
Teresa Carlomagno
EMBL
Heidelberg Germany
Martin Blackledge
Université Joseph Fourier
Grenoble France
Christian Oliver Bretschneider
Weizmann Institute
Rehovot Israel
Keri Carpenter
University of Cambridge
Cambridge UK
Frédéric Blanc
University of Liverpool
Liverpool UK
William W. Brey
National High Magnetic Field Lab / FSU
Tallahassee FL
Thomas Adrian Carpenter
University of Cambridge
Cambridge UK
John Blanchard
Helmholtz-Institut Mainz
Mainz Germany
Mark S. Brown
Arvada CO
mbrown6300@aol.com
Leah Casabianca
Clemson University
Clemson SC
bruschweiler.1@osu.edu
David Case
Rutgers University
Piscataway NJ
alexei.buevich@merck.com
Thomas Casey
University of Florida
Gainesville FL
jbunn@jeol.com
Julia Cassani
Universidad Autonoma Metropolitana
D.F Mexico
burant@unc.edu
Laura Castañar Acedo
Universitat Autónoma Barcelona
Cerdanyola del Vallés, Barcelona Spain
roberto.buratto@epfl.ch
Bethany G. Caulkins
Univ of California, Riverside
Riverside CA
jessica.burger@nist.gov
Chi Celestine
ETH, Zurich
Zurich Switzerland
darcy.burns@utoronto.ca
Yan Chang
SIBET, Chinese Academy of Sciences
Suzhou China
scott_burt@byu.edu
Fa-An Chao
National Cancer Institute
Frederick MD
Craig.Butts@bris.ac.uk
Cyril Charlier
CNRS, Ecole Normale Supérieur
Paris France
byrdra@mail.nih.gov
Mark Chaykovsky
Bruker BioSpin
Billerica MA
sheng.cai@mu.edu
Steve F. Cheatham
DuPont
Newark DE
thachcan@mit.edu
Eduard Y Chekmenev
Vanderbilt University
Nashville TN
pierrick.berruyer@ens-lyon.fr
jbierma@uci.edu
terri.bishop@spscientific.com
martin.blackledge@ibs.fr
frederic.blanc@liverpool.ac.uk
bouhraram@mail.nih.gov
rb2e12@soton.ac.uk
bowers@chem.ufl.edu
cbretsch@weizmann.ac.il
wbrey@magnet.fsu.edu
blanchard@uni-mainz.de
Rafael Bruschweiler
Ohio State University
Columbus OH
andrew.blinov@gmail.com
Alexei Buevich
Merck and Co.
Kenilworth NJ
kirill@moleculeapps.com
Jon Bunn
JEOL USA, INC.
Peabody MA
bluemich@itmc.rwth-aachen.de
Alex Burant
University of North Carolina
Chapel Hill NC
bluemler@uni-mainz.de
Roberto Buratto
EPFL SB ISIC LRMB
Lausanne Switzerland
robert.blum@yale.edu
Jessica Burger
NIST
Boulder CO
blum@uidaho.edu
Darcy Burns
University of Toronto
Toronto ON Canada
w.bocian@nil.gov.pl
Scott R Burt
Brigham Young University
Provo UT
steven.boehmer@sial.com
Craig P Butts
University of Bristol, UK
Bristol UK
kbombuwala@yahoo.com
R. Andrew Byrd
National Cancer Institute
Frederick MD
danb@ucr.edu
Sheng Cai
Marquette University
Milwaukee WI
bordonali.sim@gmail.com
Thach Can
MIT
Cambridge MA
Andrew Blinov
Higher School of Economics
Moscow Russia
Kirill Blinov
Molecule Apps
Corvallis OR
Bernhard Bluemich
RWTH Aachen University
Aachen Germany
Peter Bluemler
Institute of Physics
Mainz Germany
Robert Blum
Yale University
New Haven CT
Alexander Blumenfeld
University of Idaho
Moscow ID
Wojciech Bocian
National Medicines Institute
Warsaw Poland
Steven Boehmer
ISOTEC/Sigma-Aldrich
Miamisburg OH
Karunananda Bombuwala
International Flavors and Fragrances Inc.
Union Beach NJ
Dan Borchardt
University of California
Riverside CA
Lorenzo Bordonali
Karlsruher Institut für Technologie
Eggenstein-Leopoldshafen Germany
Frank Bosco
New Era Enterprises, Inc.
Vineland NJ
fbosco@newera-spectro.com
canetestel@gmail.com
andrea.capozzi@epfl.ch
carlomag@embl.de
klc1000@wbic.cam.ac.uk
tac12@wbic.cam.ac.uk
lcasabia@gmail.com
case@biomaps.rutgers.edu
tcasey3@chem.ufl.edu
cassani@correo.xoc.uam.mx
lauracastanar@hotmail.es
bcaul001@ucr.edu
chi.celestine@phys.chem.ethz.ch
changy@sibet.ac.cn
fa-an.chao@nih.gov
cyril.charlier@ens.fr
mark.chaykovsky@bruker.com
steve.f.cheatham@dupont.com
eduard_chekmenev@hotmail.com
Page 143
DIRECTORY OF PARTICIPANTS (as of March 31, 2015)
Banghao Chen
Florida State University
Tallahassee FL
Ouri Cohen
MGH/HST
Charlestown MA
Michael Crowley
Washington U.
Chesterfield MO
Cheng-Yu Chen
CCRC, University of Georgia
Athens GA
Kelsey Collier
UC Irvine
Irvine CA
Dongtao Cui
University of Georgia
Athens GA
Qiaoyan Chen
SIBET, CAS
Suzhou China
James Collins
University of Florida
Gainesville FL
Murali Dama
University of California, Berkeley
Berkeley CA
Yu-Wen Chen
Dpet. of Chem. & Biochem, National
Chung Cheng Uni
Chia-yi Taiwan
Kimberly L. Colson
Bruker BioSpin Corp.
Billerica MA
Joshua Damron
University of Michigan
Ann Arbor MI
Ren-Hao Cheng
Chemistry Department
Kaohsiung Taiwan
Arnaud Comment
Ecole Polytechnique
Fédérale de Lausanne
Lausanne Switzerland
Phuong Dao
University of California, Berkeley
Berkeley CA
Brian Cherry
Arizona State University
Tempe AZ
Maria Conrad Soria
University of Southern California
Pasadena CA
Brad Chmelka
UCSB
Santa Barbara CA
Gabriel A. Cook
Oklahoma State University
Stillwater OK
Min-Kyu Cho
Novartis Insts for Biomedical Research
Cambridge MA
Phillipe Corcos
Cortecnet
Mill Valley CA
Seo-Ree Choi
Gyeongsang National University
Jinju Korea
Marcy C Corey
JEOL USA, INC
Peabody MA
Yong-Geun Choi
Dept of Chemistry
Gyeongsang National University
Jinju Korea
Gabriel Cornilescu
University of Wisconsin - Madison
Madison WI
chen@chem.fsu.edu
cyc0827@uga.edu
qiaoyan@mail.ustc.edu.cn
bcde23400@gmail.com
d012020004@student.nsysu.edu.tw
brcherry@asu.edu
bradc@engineering.ucsb.edu
min-kyu.cho@novartis.com
csr29150@gmail.com
inuyonggeun@naver.com
Shidong Chu
Touro University
Vallejo CA
Shidong.Chu@tu.edu
Tatiana Churanova
Molecule Apps
Corvallis OR
tatiana.churanova@gmail.com
Deniz Cizmeciyan
Mount St. Mary's University
Los Angeles CA
dcizmeciyan@msmc.la.edu
Sarah Clark
Oregon State University
Corvallis OR
clarksar@onid.oregonstate.edu
Laurie Close
Triangle Analytical
Morrisville NC
laurie@triangleanalytical.com
Aaron Coffey
Vanderbilt University
Nashville TN
aaron.coffey@vanderbilt.edu
Helga J Cohen
University of South Carolina
Columbia SC
hjcohen0@mailbox.sc.edu
ouri@nmr.mgh.harvard.edu
kcollier@uci.edu
jhpcollins@ufl.edu
kim.colson@bruker.com
crowleym@wustl.edu
dcui@uga.edu
muralidama@berkeley.edu
jtda@umich.edu
phuong@berkeley.edu
arnaud.comment@epfl.ch
Phil Darragh
ISOTEC/Sigma-Aldrich
Miamisburg OH
mariaaco@usc.edu
Bibhuti Das
UCSD
San Diego CA
gabriel.cook@okstate.edu
Jitendra Kumar Das
CSIR - IICB
Kolkata India
pcorcos@cortecnet.com
Stephen Davidowski
Arizona State University
Tempe AZ
mcorey@jeol.com
Ben Davis
Vernalis R&D Ltd
Cambridge UK
gabrielc@nmrfam.wisc.edu
Anna de Angelis
UC San Diego
La Jolla CA
corzilius@em.uni-frankfurt.de
Chris Dean
ISOTEC/Sigma-Aldrich
Miamisburg OH
samuel.cousin@ens.fr
Federico del Rio
Institute of Chemistry, UNAM
Mexico Mexico
andrew@magritek.com
Frank Delaglio
Santa Clara CA
Björn Corzilius
Goethe University
Frankfurt am Main Germany
Samuel Cousin
Ecole Normale Supérieure Paris
Paris France
Andrew Coy
Magritek Limited
Wellington New Zealand
Levi Craft
Bucknell University
Lewisburg PA
phil.darragh@sial.com
bdas@ucsd.edu
jkdas.iicb@gmail.com
sdavidow@asu.edu
b.davis@vernalis.com
adeangel@ucsd.edu
christopher.dean@sial.com
federico.delrio@gmail.com
delaglio@nmrscience.com
dlc030@bucknell.edu
John Delayre
Tecmag
Houston TX
bcrane3@jhu.edu
Michael Delk
University of Pittsburgh
Pittsburgh PA
cross@rototec.com
Karolien Denef
Colorado State University
Fort Collins CO
cross@magnet.fsu.edu
Sandrine Denis-Quanquin
Laboratoire de Chimie - ENSL
Lyon France
roncrouch@mac.com
Dan Dennehy
Cambridge Isotope Lab
Tewksbury MA
Ben Crane
Johns Hopkins University
Baltimore MD
David Cross
Wilmad-LabGlass
Vineland NJ
Timothy A. Cross
Natl High Magnetic Field Lab
Tallahassee FL
Ron Crouch
JEOL USA
Peabody MA
jld@tecmag.com
mid15@pitt.edu
Karolien.Denef@Colostate.edu
sandrine.denis-quanquin@ens-lyon.fr
ddennehy@isotope.com
Page 144
DIRECTORY OF PARTICIPANTS (as of March 31, 2015)
Philip R Dennison
UC Irvine
Irvine CA
Joe Dumais
Boise State University
Boise ID
Steven Donald Emerson
Resonance Consulting
Milan MI
Basant Dhital
CUNY Graduate Center
New York NY
Jean-Nicolas Dumez
ICSN - CNRS
Gif-sur-Yvette France
Earl Emery
Tecmag, Inc.
Houston TX
Shangwu Ding
Natl Sun Yat-sen Univ
Kaohsiung Taiwan
Olivier Duss
The Scripps Research Institute
San Diego CA
Robert A DiPasquale
JEOL USA, INC
Peabody MA
Jeff Duyn
NIH
Bethesda MD
oduss@scripps.edu
Meike Emondts
Institut für Technische und
Makromolekulare Chemie
Aachen Germany
Piotr Dobrowolski
University of Kentucky
Lexington KY
Cecil Dybowski
University of Delaware
Newark DE
jhd@helix.nih.gov
James W. Emsley
University of Southampton
Southampton UK
Fulya Dogan
Argonne National Laboratory
Lemont IL
Margaret A. Eastman
Oklahoma State University
Stillwater OK
dybowski@udel.edu
Frank Engelke
Bruker Biospin
Rheinstetten Germany
Michael Doligalski
University of South Florida
Tampa FL
Hugh Eaton
Merck Research Labs
Kenilworth NJ
meastman@chem.okstate.edu
Raul G. Enríquez
Instituto de Química, UNAM
México Mexico
Santi Dominguez
Mestrelab Research
Santiago De Compostela, A Coruna
Spain
Arthur Edison
UF/NHMFL
Gainesville FL
hugh.eaton@merck.com
Firealem Erko
Ambo University
Ambo Ethiopia
aedison@ufl.edu
Nan Eshuis
Radboud University
Nijmegen The Netherlands
dennis.edwards@utah.edu
Andy Evans
Drew University
Mendham NJ
cedric.eichmann@phys.chem.ethz.ch
Arjang Fahim
University of South Carolina
Columbia SC
stei0464@umn.edu
Amr F. Fahmy
Harvard Medical School
Boston MA
Eliav@post.tau.ac.il
Alexander Falk
USC
Pasadena CA
charity.elifritz@sial.com
Alexandra Faucher
University of Alberta
Edmonton AB Canada
kelliot8@uwyo.edu
Franck Fayon
CEMHTI - CNRS
Orleans France
paul@dotynmr.com
Jasna Fejzo
Novartis Institutes for Biomedical Rsrch
Cambridge MA
stefan.elrington@yale.edu
Isabella C. Felli
CERM University of Florence
Sesto Fiorentino Italy
malathy@ufl.edu
Yesu Feng
UCSF
San Francisco CA
dennison@uci.edu
bdhital@gc.cuny.edu
ding@mail.nsysu.edu.tw
dipas@jeol.com
piotr.d@uky.edu
fdogan@anl.gov
mdoligalski@mail.usf.edu
josephdumais@boisestate.edu
jeannicolas.dumez@cnrs.fr
sdominguez@mestrelab.com
Dennis S. Edwards
University of Utah
Salt Lake City UT
donovan@unl.edu
Cedric Eichmann
ETH Zurich
Zurich Switzerland
david@dotynmr.com
Samuel Einstein
University of Minnesota
Minneapolis MN
glenn@dotynmr.com
Uzi Eliav
School of Chemistry, Tel Aviv University
Tel Aviv Israel
judy@dotynmr.com
Charity Elifritz
Isotec/Sigma Aldrich
Miamisburg OH
justindouglas@ku.edu
Korth Elliott
University of Wyoming
Laramie WY
melanie.e.drake@gmail.com
Paul Ellis
Doty Scientific
Columbia SC
donnad@isotope.com
Stefan Elrington
Yale University
New Haven CT
dubroca@magnet.fsu.edu
Malathy Elumalai
McKnight Brain Institute,Univ of Florida
Gainesville FL
Beth Donovan
University of Nebraska
Lincoln NE
F. David Doty
Doty Scientific
Columbia SC
Glenn Doty
Doty Scientific, Inc.
Columbia SC
Judy Doty
Doty Scientific, Inc.
Columbia SC
Justin Douglas
University of Kansas - NMR Lab
Lawrence KS
Melanie Drake
UC Berkeley
Berkeley CA
Donna Drakoulakos
Cambridge Isotope Labs
Tewksbury MA
Thierry Dubroca
National High Magnetic Field Laboratory
Tallahassee FL
Venkat Dudipala
University Of Akron
Akron OH
vrd@uakron.edu
Melinda Duer
Cambridge Univ.
Cambridge UK
mjd13@cam.ac.uk
don.emerson@comcast.net
emery@tecmag.com
Emondts@itmc.rwth-aachen.de
jwe@soton.ac.uk
frank.engelke@bruker.com
enriquezhabib@gmail.com
firealemg@yahoo.com
n.eshuis@science.ru.nl
andy.evans@verizon.net
fahim@email.sc.edu
amr_fahmy@hms.harvard.edu
sandyfalk@gmail.com
alexandra.faucher@ualberta.ca
franck.fayon@cnrs-orleans.fr
jasna.fejzo@novartis.com
felli@cerm.unifi.it
ysduke@gmail.com
Gianni Ferrante
Stelar s.r.l.
Mede (PV) Italy
ferrante@stelar.it
Page 145
DIRECTORY OF PARTICIPANTS (as of March 31, 2015)
Helen Ferreira
University of Washington
Seattle WA
Riqiang Fu
National High Magnetic Field Laboratory
Tallahassee FL
Ion Ghiviriga
University of Florida
Gainesville FL
John Ferruzzi
Wilmad Lab Glass
Vineland NJ
Kazuo Furihata
University of Tokyo
Tokyo Japan
Ranajeet Ghose
The City College of New York
New York NY
David Flores Solis
Instituto de Química UNAM
México Mexico
George Furst
University of Pennsylvania
Philadelphia PA
Andrew Gibbs
Bruker UK Ltd
Coventry UK
Pierre Florian
CEMHTI-CNRS
Orleans Cedex 2 France
Boris Fürtig
Goethe University
Frankfurt Germany
Roberto R. Gil
Carnegie Mellon University
Pittsburgh PA
Peter F. Flynn
Univ of Utah
Salt Lake City UT
Michael M. Fuson
Denison University
Granville OH
Michelle Gill
National Cancer Institute
Frederick MD
Frank H. Foersterling
Univ. of Wisconsin - Milwaukee
Milwaukee WI
Manjunatha Reddy G N
University of Warwick
Coventry UK
Nicolas Giraud
Universite Paris-Sud
Orsay France
Shelby Follett
University of Wyoming
Laramie WY
Neal Gallagher
Nanalysis Corp
Calgary AB Canada
Patrick Giraudeau
Université de Nantes
Nantes Cedex 03 France
Alexander Forse
University of Cambridge
Cambridge UK
Zhehong Gan
NHMFL
Tallahassee FL
Simon Glanzer
University of Graz / Institute of Chemistry
Graz Styria Austria
Blythe Fortier-McGill
University of Toronto
Toronto ON Canada
Qi Gao
Complex Carbohydrate Research Center
Athens GA
Steffen Glaser
Technical Univ. Munich
Garching Germany
C. Andrew Fowler
University of Iowa
Iowa City IA
Xinfeng Gao
Indiana University
Bloomington IN
Alexei Glebov
OptiGrate Corp.
Orlando FL
Don Frank
Open Technologies, Inc.
Granger IN
Marie Alexis Garcia
Mount Saint Mary's University
Los Angeles CA
John Glushka
University of Georgia
Athens GA
Jonas Fredriksson
Gothenburg University
Gothenburg Sweden
David Gardner
MR Resources
Fitchburg MA
Miriam Gochin
Touro University California
Vallejo CA
Amy Freund
Bruker BioSpin
Billerica MA
Michael Garwood
University of Minnesota
Minneapolis MN
Steffen Goerke
German Cancer Research Center
Heidelberg Germany
Merideth Frey
Princeton University
Princeton NJ
Xinmin Ge
China University of Petroleum
Qingdao China
Amir Goldbourt
Tel Aviv University
Tel Aviv Israel
Michael Frey
JEOL USA, INC
Peabody MA
Teklab Gebregiworgis
University of Nebraska-Lincoln
Lincoln NE
Sergey Golotvin
ACD/ Labs
Moscow Russia
Josh Friedman
AAAS
Washington DC
Leslie Gelbaum
Georgia Tech
Atlanta GA
Muller Gomes
University of California, Berkeley
Berkeley CA
Dominique Frueh
Johns Hopkins School of Medicine
Baltimore MD
Ioannis Gelis
Univ of South Florida, Chemistry
Tampa FL
Gil Goobes
Bar Ilan University
Ramat Gan Israel
Lucio Frydman
Weizmann Institute
Rehovot Israel
Rex Gerald
Missouri Univ of Science and Tech
Rolla MO
Jeremy Good
Cryogenic Ltd
London UK
hfbuckeye@gmail.com
john.ferruzzi@wilmad-labglass.com
qdavidf@gmail.com
pierre.florian@cnrs-orleans.fr
peter.flynn@utah.edu
holger@uwm.edu
sfollet1@uwyo.edu
alexforse1@gmail.com
blythe.fortier.mcgill@utoronto.ca
andrew-fowler@uiowa.edu
donfrank@opentech.biz
jonas.mb@gmail.com
Amy.Freund@bruker.com
mfrey@princeton.edu
frey@jeol.com
josh.nmr@gmail.com
dfrueh1@jhmi.edu
lucio.frydman@weizmann.ac.il
Page 146
rfu@magnet.fsu.edu
afuriha@mail.ecc.u-tokyo.ac.jp
furst@sas.upenn.edu
fuertig@nmr.uni-frankfurt.de
fuson@denison.edu
gnm.reddy@warwick.ac.uk
neal.gallagher@nanalysis.com
gan@magnet.fsu.edu
qigao@uga.edu
xgao@indiana.edu
marigarc1512@mymsmc.la.edu
davidgardner@mrr.com
gar@cmrr.umn.edu
gexinmin2002@163.com
teklab@huskers.unl.edu
lg2@prism.gatech.edu
igelis@usf.edu
geraldr@mst.edu
ion@chem.ufl.edu
rghose@sci.ccny.cuny.edu
andrew.gibbs@bruker.com
rgil@andrew.cmu.edu
michelle.gill@nih.gov
nicolas.giraud@u-psud.fr
patrick.giraudeau@univ-nantes.fr
simon.glanzer@uni-graz.at
glaser@tum.de
aglebov@optigrate.com
glushka@uga.edu
miriam.gochin@tu.edu
s.goerke@dkfz.de
amirgo@post.tau.ac.il
golotvin@acdlabs.ru
muller.gomes@berkeley.edu
ggoobes@hotmail.com
jeremy@cryogenic.co.uk
DIRECTORY OF PARTICIPANTS (as of March 31, 2015)
Boyd M. Goodson
Southern Illinois University
Carbondale IL
Jerry Jin Guo
UC Irvine
Irvine CA
Kikuko Hayamizu
University of Tsukuba
Tsukuba Japan
David Goodwin
University of Southampton
Southampton UK
Michael Habeck
University of Göttingen
Göttingen Germany
Sophia E. Hayes
Washington University
Saint Louis MO
Peter L. Gor'kov
National High Magnetic Field Laboratory
Tallahassee FL
Ibraheem Haies
University of Southampton
Southampton UK
Brett Haywood
Technology Consultancy Services
Leicester UK
Benjamin Görling
KIT
Karlsruhe Germany
Kathleen Hall
Washington Univ Med Sch
Saint Louis MO
Yiyong He
The Dow Chemical Company
Midland MI
Alvar Gossert
Novartis Institutes for Biomedical Rsrch
Basel Switzerland
Blake Hammann
Washington University
St. Louis MO
Henrike Heise
Heinrich Heine Universität Düsseldorf
Düsseldorf Germany
G. A. Nagana Gowda
University of Washington
Seattle WA
Shellie Hammond
MR Resources
Fitchburg MA
Leah Heist
UNC Chapel Hill
Chapel Hill NC
Hanna Gracz
NMR Facility, NCSU
Raleigh NC
Kee Sung Han
Pacific Northwest National Laboratory
Richland WA
Gonzalo Hernández
Vis Magnetica
Montevideo Uruguay
Stephan Grage
Karlsruhe Institute of Technology
Karlsruhe Germany
stephan.grage@kit.edu
Oc Hee Han
Weatern Seoul Center
Korea Basic Science Institut
Seoul Korea
Adam Hill
Pfizer
Kalamazoo MI
grandinetti.1@osu.edu
Song-I Han
University of California Santa Barbara
Santa Barbara CA
prgraupner@dow.com
D. Flemming Hansen
ISMB, Univ. College London
London UK
george.gray.nmr@gmail.com
Rick Hapanowicz
Quantum Design
San Diego CA
rgg@mit.edu
Jay Harkins
Kimble Chase
Rockwood TN
amg100@pitt.edu
Jim Harper
University of Central Florida
Orlando FL
jungu@sas.upenn.edu
Arnold Harrison
Rampant Technology Partners, LLC
South Charleston WV
mgu@stanford.edu
Jerry Hatvany
Triangle Analytical, Inc.
Morrisville NC
bgoodson@chem.siu.edu
d.goodwin@soton.ac.uk
pgorkov@magnet.fsu.edu
benjamin.goerling@kit.edu
alvar.gossert@novartis.com
ngowda@uw.edu
hanna_gracz@ncsu.edu
Philip Grandinetti
The Ohio State University
Columbus OH
Paul R Graupner
Dow AgroSciences
Indianapolis IN
George Gray
Retired
Portola Valley CA
Robert Griffin
MIT
Cambridge MA
Angela Gronenborn
University of Pittsburgh
Pittsburgh PA
Jun Gu
University of Pennsylvania
Philadelphia PA
Meng Gu
Radiology, Stanford University
Stanford CA
Xudong Guan
University of Illinois at UrbanaChampaign
Urbana IL
xdguan@illinois.edu
superjerry_guo@hotmail.com
mhabeck@gwdg.de
imh7821@yahoo.com
kathleenhal@gmail.com
blake.hammann@wustl.edu
Shellie@mrr.com
keesung.han@pnnl.gov
brett.haywood@nottingham.ac.uk
Yhe@dow.com
hakkaeiessee1@gmail.com
lheist@unc.edu
gonzalo@vismagnetica.com
adam.c.hill@pfizer.com
Sebastian Hiller
Biozentrum
Basel Switzerland
songi@chem.ucsb.edu
Jerry Hirschinger
Purdue University
West Lafayette IN
d.hansen@ucl.ac.uk
David Hirsh
University of Windsor
Windsor ON Canada
rickh@qdusa.com
Iyat Hissin
BelArt / SP Industries
Stone Reidge NY
s.collins@kimble-change.com
Jeffrey C. Hoch
Univ of Connecticut Health Ctr
Farmington CT
James.Harper@ucf.edu
Casper Hoeck
Technical University of Denmark
Kgs. Lyngby Denmark
arnold.harrison@pobox.com
Peter Hoefer
Bruker Biospin
Rheinstetten Germany
jerry@triangleanalytical.com
Jens Höfflin
Lab of Simulation - University of Freiburg
Freiburg Germany
erhard.haupt@uni-hamburg.de
Heike Hofstetter
University of Wisconsin - Madison
Madison WI
bhausmann@berkeley.edu
Gregory Holland
San Diego State University
San Diego CA
Erhard T.K. Haupt
Dept Chemistry, University Hamburg
Hamburg Germany
Birgit Hausmann
LBNL
Kensington CA
Terry Gullion
West Virginia University
Morgantown WV
Bruce Hawkins
Ft. Collins CO; Cohasset MN
Fort Collins CO
terry.gullion@mail.wvu.edu
hayes@wustl.edu
ohhan@kbsi.re.kr
Farhana Gul-E-Noor
Brooklyn College of CUNY
Brooklyn NY
gnfarhana@gmail.com
hayamizu.k3@gmail.com
pct@pctnmr.com
sebastian.hiller@unibas.ch
jerryh56@purdue.edu
hirsh@uwindsor.ca
ihissin@belart.com
hoch@uchc.edu
casho@kemi.dtu.dk
peter.hoefer@bruker.com
hoefflin@imtek.de
hofstetter@chem.wisc.edu
gholland@mail.sdsu.edu
Page 147
DIRECTORY OF PARTICIPANTS (as of March 31, 2015)
Laura Holte
Doty Scientific, Inc.
Columbia SC
laura@dotynmr.com
Mitsu Ikura
Princess Margaret Cancer Centre,
University Health
Toronto ON Canada
ghu002@ucr.edu
Andrew Ilott
New York University
New York NY
hu_haitao@lilly.com
Shunsuke Imai
Havard Medical School
Boston MA
jghu@mrl.ucsb.edu
Mario Incitti
Phoenix NMR LLC
Fort Collins CO
Jianzhi.Hu@pnnl.gov
Stacey Ira
Mount St. Mary's University
North Hills CA
hujunfsu@gmail.com
Boris Itin
NYSBC
New York NY
Mary.Hu@pnnl.gov
Arnold Itkin
NMR Assoc.
Fitchburg MA
whu@coh.org
Monika Ivancic
University of Vermont
Burlington VT
huang@chemistry.harvard.edu
Wolfgang Jahnke
Novartis Institutes for Biomedical Rsrch
Basel Switzerland
huhns@onid.oregonstate.edu
Sami Jannin
EPFL
Lausanne Switzerland
Guoxiang Hu
University of California Riverside
Riverside CA
Haitao Hu
Eli Lilly and Company
Indianapolis IN
Jerry Hu
Univ of California
Santa Barbara CA
Jian Zhi Hu
Pacific Northwest National Laboratory
Richland WA
Jun Hu
AstraZeneca
Waltham MA
Mary Yang Hu
Pacific Northwest National Laboratory
Richland WA
Weidong Hu
City of Hope
Duarte CA
Shaw Huang
Harvard University
Cambridge MA
Stephen Huhn
Oregon State University
Corvallis OR
Alan Hume
Bruker BioSpin
Billerica MA
alan.hume@bruker.com
Ivan Hung
NHMFL
Tallahassee FL
hung@magnet.fsu.edu
Ralph Hurd
GE Healthcare
Menlo Park CA
Fangling Ji
DLUT
Dalian China
andyilott@gmail.com
Boban John
Thermo Fisher Scientific
Fremont CA
shunsuke_imai@hms.harvard.edu
Eric C Johnson
Bruker Biospin
Fremont CA
mi@phoenixnmr.com
LeRoy Johnson
Retired
Cupertino CA
stacira@mymsmc.la.edu
Paul Jonsen
Revolution NMR / TalaveraScience
Harrogate UK
bitin@nysbc.org
Antoni Jurkiewicz
University of Chicago
Chicago IL
info@nmr-associates.com
Mike Kaiser
California State University at Northridge
Northridge CA
Monika.Ivancic@uvm.edu
Lazaros T Kakalis
Rutgers University
Newark NJ
wolfgang.jahnke@novartis.com
Babis Kalodimos
Rutgers University
Piscataway NJ
sami.jannin@epfl.ch
Ilia Kaminker
UCSB
Santa Barbara CA
Lukasz Jaremko
Deutsches Zentrum für
Neurodegenerative Erkrankung
Goettingen Germany
jaremko@gmail.com
Mariusz Jaremko
Max-Planck-Institut für
Biophysikalische Chemie
Goettingen Germany
ajurkiew@uchicago.edu
john.kaiser@csun.edu
kakalis@andromeda.rutgers.edu
babis@rutgers.edu
ilia.kaminker@gmail.com
Paul Kanyha
Tecmag
Houston TX
info@tecmag.com
jaroniec.1@osu.edu
j.jarvis@soton.ac.uk
Derrick Kaseman
University of California
Davis CA
jenkinh@mcmaster.ca
Singh Kawarpal
RWTH Aachen University
Aachen Germany
jaekyun.jeon@gmail.com
Eric Keeler
Francis Bitter Magnet Lab and MIT
Cambridge MA
illyun@hotmail.com
Hilary Jenkins
McMaster University
Hamilton ON Canada
sven_hyberts@hms.harvard.edu
Jaekyun Jeon
University of Central Florida
Orlando FL
Page 148
paul.jonsen@talaverascience.com
Magnus Karlsson
Albeda Research
Copenhagen Denmark
dennis.w.hwang@gmail.com
midso@umail.ucsb.edu
13carbon@gmail.com
mjaremko@ucsd.edu
James Jarvis
University of Southampton
Southampton UK
Matthew Idso
University of California
Santa Barbara CA
eric.johnson@bruker.com
Rob Kaptein
Utrecht University
Utrecht The Netherlands
Christopher P. Jaroniec
The Ohio State University
Columbus OH
Sven G. Hyberts
Harvard Medical School
Boston MA
boban.john@thermofisher.com
antypater@gmail.com
lilyimscrump@gmail.com
Ryeo yun Hwang
Chungnam National University
Yuseong-gu Korea
fanglingji@gmail.com
Mohammed Kaplan
Universiteit Utrecht
Utrecht The Netherlands
Matt Jaremko
UCSD
La Jolla CA
Dennis Hwang
Dpet. of Chem. & Biochem
National Chung Cheng Univ
Chia-Yi Taiwan
doas1mind@berkeley.edu
mikura@uhnresearch.ca
ralph.hurd@ge.com
Tung Husanli
National Chung Cheng University
Chia-yi Taiwan
Keunhong Jeong
UC Berkeley
Berkeley CA
m.kaplan@uu.nl
r.kaptein@uu.nl
magnus.karlsson@albeda.dk
kaseman.7@gmail.com
singh@itmc.rwth-aachen.de
egkeeler@mit.edu
DIRECTORY OF PARTICIPANTS (as of March 31, 2015)
James H Keeler
University of Cambridge
Cambridge UK
Takeshi Kobayashi
Iowa State University
Ames IA
Till Kuehn
Bruker Biospin AG
Fällanden Switzerland
Tony W. Keller
Bruker BioSpin
Rheinstetten Germany
Herbert Kogler
University of Bremen
Schlossborn Germany
Rainer Kuemmerle
Bruker BioSpin
Fällanden Switzerland
John Kelly
Department of Chemistry, UCI
Irvine CA
Christopher L Kojiro
University of Michigan
Ann Arbor MI
Kristin Kumashiro
University of Hawaii
Honolulu HI
Rime Kerfah
NMR-Bio Structural Biology Institute
Grenoble France
Fangming Kong
Pfizer
Groton CT
Georg Künze
University of Leipzig
Leipzig Germany
Baris Key
Argonne National Laboratory
Lemont IL
Martin Koos
Karlsruhe Institute of Technology
Eggenstein-Leopoldshafen Germany
Eriks Kupce
Bruker Biospin
Coventry UK
Ken Kezeor
Open Technologies, Inc.
Granger IN
Sophie Koroloff
North Carolina State University
Raleigh NC
Ilya Kuprov
University of Southampton
Southampton UK
Domarin Khago
Dept of Chemistry, University of
California
Irvine CA
Jan Korvink
Karlsruhe Institite of Technology
Eggenstein-Leopoldshafen Germany
Gonemon Kurihara
JEOL Ltd.
Akishima Tokyo Japan
dkhago@uci.edu
Janusz Koscielniak
FNLCR
Frederick MD
Anna Kuznetsova
Air Force Research Laboratory (AFRL)
Eglin AFB FL
purnima.khandelwal@bms.com
Samuel Kotler
University of Michigan
Ann Arbor MI
Gary Larson
Silantes GmbH
Munich Germany
clkhetrapal@hotmail.com
Katalin E. Kover
University of Debrecen
Debrecen Hungary
Frank Laukien
Bruker
Billerica MA
dkiemle@esf.edu
Nkozlyuk Kozlyuk
Dept of Chemistry, University of
California
Irvine CA
Tanguy Le Marchand
ISA Université de Lyon
Lyon France
jhk10@cam.ac.uk
tony.keller@bruker-biospin.de
kellyj2@uci.edu
rime.kerfah@ibs.fr
bkey@anl.gov
ken@kezeor.com
Purnima Khandelwal
Bristol-Myers Squibb Company
Princeton NJ
CL Khetrapal
Center of Biomedical Research
Lucknow India
David Kiemle
SUNY ESF
Syracuse NY
Takanori Kigawa
RIKEN Quantitative Biology Center
(QBiC)
Yokohama Japan
kigawa@riken.jp
Hai-Young Kim
Merck Research Laboratories
Kenilworth NJ
takeshi@iastate.edu
herbert.kogler@t-online.de
ckojiro@umich.edu
fangming.kong@pfizer.com
martin.koos@kit.edu
snkorolo@ncsu.edu
jan.korvink@kit.edu
koscieja@mail.nih.gov
kotlesam@umich.edu
kover@science.unideb.hu
till.kuehn@bruker.com
Rainer.kuemmerle@bruker.ch
kumashir@hawaii.edu
Georg.Kuenze@medizin.uni-leipzig.de
eriks.kupce@bruker.co.uk
i.kuprov@soton.ac.uk
gkurihar@jeol.co.jp
kuznetsova.ann@gmail.com
sebastian.schmidt@silantes.com
Frank.Laukien@bruker-biospin.com
tanguy.le_marchand@ens-lyon.fr
nkozlyuk@uci.edu
Alisa Leavesley
University of California, Santa Barbara
Santa Barbara CA
chempacker@gmail.com
Krish Krishnamurthy
Chempacker LLC
San Jose CA
aleavesley@chem.ucsb.edu
hai-young.kim@merck.com
Shilpa Krishnan
Mount Saint Mary's University
La Palma CA
Lauriane Lecoq
Département de Biochimie et Médecine
Moléculaire
Montreal QC Canada
kimhn10@kbsi.re.kr
Ashok Krishnaswami
JEOL USA, INC
Peabody MA
Michael Ledwig
Pure Devices GmbH
Wurzburg Germany
jpking@berkeley.edu
Chris Kroenke
OHSU
Portland OR
Ae-Ree Lee
Gyeongsang National University
Jinju Korea
bob_kinsey@goodyear.com
Bashar Ksebati
Wayne State University
Detroit MI
Chia-Ying Lee
National Chung Cheng University
Chia-yi Taiwan
kisss@imtek.uni-freiburg.de
Vojtech Kuban
Masaryk University, CEITEC
Brno Czech Republic
David Lee
UC San Diego
La Jolla CA
kitchen@magnet.fsu.edu
Ryan Kudla
University of California, Riverside
Riverside CA
Hsiau-Wei Lee
University of California, Santa Cruz
Santa Cruz CA
Hyun Na Kim
Korea Basic Science Institute
Seoul Korea
Jonathan P King
Dept of Chemistry, University of
California
Berkeley CA
Robert Kinsey
Goodyear Tire & Rubber Company
Akron OH
Sebastian Z. Kiss
University of Freiburg - IMTEK
Freiburg Germany
Jason Kitchen
National High Magnetic Field Laboratory
Tallahassee FL
shilkris@mymsmc.la.edu
ashok@jeol.com
kroenkec@ohsu.edu
bksebati@chem.wayne.edu
236585@mail.muni.cz
rkudl001@ucr.edu
lauriane.lecoq@umontreal.ca
michael.ledwig@pure-devices.com
dldofl24@gmail.com
natural77111@gmail.com
djl002@ucsd.edu
hlee74@ucsc.edu
Page 149
DIRECTORY OF PARTICIPANTS (as of March 31, 2015)
Jaehyuk Lee
MD Anderson Cancer Center
Houston TX
Ilya Litvak
Florida State University/NHMFL
Tallahassee FL
Thorsten Maly
Bridge12 Technologies, Inc.
Framingham MA
Jae-Seung Lee
New York University
New York NY
David H. Live
University of Georgia/CCRC
Athens GA
John Mamin
IBM Almaden Research Center
San Jose CA
Joon-Hwa Lee
Gyeongsang National University
Jinju Korea
Nikolaus M. Loening
Lewis & Clark College
Portland OR
Jung Ho Lee
National Institutes of Health
Bethesda MD
Richard Lois
JEOL USA
Peabody MA
loening@lclark.edu
Daniele Mammoli
École Polytechnique Fédérale de
Lausanne
Lausanne Switzerland
Avigdor Leftin
Memorial Sloan Kettering
New York NY
Joanna R. Long
University of Florida
Gainesville FL
lois@jeol.com
Stan Manatt
Caltech
La Canada CA
Maureen Leninger
New York University
New York NY
Andrew Longhini
University of Maryland, College Park
Washington DC
jrlong@mbi.ufl.edu
Suraj Manrao
Stable Isotope Consulting Group
Old Bridge NJ
Eric Leonardis
Bruker Biospin
Wissembourg France
J. Patrick Loria
Yale University
New Haven CT
longhini@umd.edu
Kanmi Mao
ExxonMobil
Clinton NJ
Mathilde Lerche
Albeda Research
Copenhagen Denmark
Justin Lorieau
U Illinois, Chicago
Chicago IL
patrick.loria@yale.edu
Lauren Marbella
University of Pittsburgh
Pittsburgh PA
Anne Lesage
CNRS
Villeurbanne France
Guillermo Lucena
University of Sussex
Brighton UK
jlorieau@uic.edu
Alexander Marchanka
EMBL
Heidelberg Germany
Garett Leskowitz
Nanalysis Corp.
Calgary AB Canada
Alicia Lund
UC Santa Barbara
Santa Barbara CA
guillermolucena@hotmail.com
Carla Marchioro
R4R -Research for Rent
Villafranca di Verona Italy
Hoi Tik Alvin Leung
University of Basel
Basel Switzerland
Rensheng Luo
University of Missouri St Louis
St Louis MO
asmith@chem.ucsb.edu
Irene Marco-Rius
UCSF
San Francisco CA
Shi Li
Quantum Design
San Diego CA
Burkhard Luy
KIT
Karlsruhe Germany
luor@umsl.edu
John P. Marino
IBBR-NIST
Rockville MD
Yang Li
MUSC
Charleston SC
Werner E. Maas
Bruker
Billerica MA
Burkhard.Luy@kit.edu
Malgorzata Marjanska
CMRR, University of Minnesota
Minneapolis MN
Yi-Xin Li
Bristol-Myers Squibb Co.
Pennington NJ
Alviclér Magalhães
SpinCore
Rio de Janeiro Brazil
Werner.Maas@bruker.com
John L. Markley
University of Wisconsin-Madison
Madison WI
Yalda Liaghati Mobarhan
University of Toronto
Toronto ON Canada
Brendan Mahoney
University of Notre Dame
Notre Dame IN
alvicler@gmail.com
Brian L. Marquez
Mestrelab Research
Santiago de Compostela Spain
Chia-Cheng Lin
Shigemi, Inc.
Allison Park PA
Subhabrata Majumder
SUNY Albany
Albany NY
bmahone3@nd.edu
Dick Marsh
DMIS/NMR Assoc.
Fitchburg MA
Jessica Lin
Shigemi, Inc.
Allison Park PA
Arthur Maknenko
University of South Florida
Tampa FL
smajumder@albany.edu
Laura Martel
JRC-ITU
Eggenstein Leopoldshafen Germany
Rasmus J. Linser
Max Planck Institute BPC
Göttingen Germany
Nikita Malik
Indian Institute of Technology Bombay
Mumbai India
amaknenk@mail.usf.edu
Michele Martin
UC Davis
Davis CA
nikitamalik@iitb.ac.in
Rachel W. Martin
UC Irvine
Irvine CA
l.jaehyuk@gmail.com
jaeseung.lee@nyu.edu
joonhwa@gnu.ac.kr
jungho.lee@nih.gov
avigdorleftin@gmail.com
ml3662@nyu.edu
eric.leonardis@bruker.com
mathilde.lerche@albeda.dk
Anne.Lesage@ens-lyon.fr
leskowitz@nanalysis.com
alvin.leung@unibas.ch
sli@qdusa.com
liyyan@musc.edu
yixin.li@bms.com
y.liaghati@mail.utoronto.ca
custserv@shigeminmr.com
custserv@shigeminmr.com
rasmus.linser@gmx.de
Page 150
ilya.litvak@gmail.com
dlive@ccrc.uga.edu
tmaly@bridge12.com
mamin@us.ibm.com
daniele.mammoli@epfl.ch
manatt@ktb.net
surajmanra@aol.com
kanmi.mao@exxonmobil.com
lem64@pitt.edu
marchank@embl.de
marchioro.carla@alice.it
irene.marco-rius@ucsf.edu
john.marino@nist.gov
gosia@cmrr.umn.edu
markley@nmrfam.wisc.edu
brian@mestrelab.com
dmisnmr@gmail.com
lpm.martel@gmail.com
mnmartin@ucdavis.edu
rwmartin@uci.edu
DIRECTORY OF PARTICIPANTS (as of March 31, 2015)
Guillaume Mas
Structural Biology Institute
Grenoble France
Jaclyn Metropolit
Nanalysis Corp
Calgary AB Canada
Eric Moore
LCP, NIDDK, National Insitutes of Health
Bethesda MD
Francesca Massi
University of Massachusetts
Worcester MA
Kenneth Metz
Boston College
Chestnut Hill MA
Adolfo Moraes
Federal University of Rio de Janeiro
Rio de Janeiro Brazil
Shinichi Masuzawa
JEOL
Tokyo Japan
Carl A. Michal
University of British Columbia
Vancouver BC Canada
Steven Morgan
Brooklyn College of CUNY
Brooklyn NY
Gheorghe Mateescu
Case Western Reserve University
Cleveland OH
Ryszard Michalczyk
Los Alamos National Laboratory
Los Alamos NM
Martha Morton
University of Nebraska - Lincoln
Lincoln NE
Yoh Matsuki
Osaka University
Suita Japan
Emeric Miclet
Univ. Pierre et Marie Curie
Paris France
Beth Moscato
Yale University
New Haven CT
Tatsuya Matsunaga
Kyoto University
Kyoto-shi Japan
Matthew Miele
Bucknell University
Lewisburg PA
Arvin Moser
ACD/ Labs
Toronto ON Canada
Eugene Mazzola
University of Maryland
College Park MD
emazzola@umd.edu
Pascal Mieville
Ecole Polytechnique Fédérale de
Lausanne
Lausanne Switzerland
Kamal Mroue
University of Michigan
Ann Arbor MI
mccals@rpi.edu
Bozhana P Mihkova
Bulgarian Academy of Sciences
Sofia Bulgaria
crmccullough@mdanderson.org
Kevin Millis
Cambridge Isotope Labs, Inc.
Andover MA
ryan.mckay@ualberta.ca
Jill Millstone
University of Pittsburgh
Pittsburgh PA
stephen.mckenna@ineos.com
Eugene Milshteyn
UCSF
San Francisco CA
laura.mcwade@gmail.com
Mark J Milton
Takeda
Cambridge MA
bruna.campos@lnbio.cnpem.br
Virginia Miner
Acorn NMR
Livermore CA
garymeints@missouristate.edu
Prasanna Mishra
Mayo Foundation
Rochester MN
markus@marmei.net
Takashi Mizuno
JEOL
Kyoto Japan
guillaume.mas@gmail.com
francesca.massi@umassmed.edu
masuzawa@jeol.co.jp
gdm2@case.edu
yoh@protein.osaka-u.ac.jp
matsunaga@kuchem.kyoto-u.ac.jp
Scott A. McCallum
Rensselaer Polytechnic Institute
Troy NY
Christopher McCullough
M.D. Anderson Cancer Center
Houston TX
Ryan McKay
Chemistry - Univ. of Alberta
Edmonton AB Canada
Steve McKenna
Ineos Technologies
Naperville IL
Laura McWade
UC Davis
Davis CA
Bruna Medéia de Campos Ramos
LNBio
Campinas Brazil
Gary A. Meints
Missouri State
Springfield MO
Markus Meissner
IMT, Karlsruhe Institute of Technology
Eggenstein-Leopoldshafen Germany
Giuseppe Melacini
McMaster University
Hamilton ON Canada
melacin@mcmaster.ca
Tyler Meldrum
The College of William and Mary
Williamsburg VA
jackie.metropolit@nanalysis.com
kenneth.metz@bc.edu
michal@physics.ubc.ca
rmichalczyk@lanl.gov
emeric.miclet@upmc.fr
mmm051@bucknell.edu
adolfofisica@gmail.com
smorgan@brooklyn.cuny.edu
mmorton4@unl.edu
beth.moscato@yale.edu
arvin.moser@acdlabs.com
mrouek@umich.edu
pascal.mieville@epfl.ch
Leonard J Mueller
University of California, Riverside
Riverside CA
mikhova@yahoo.com
Dwaipayan Mukhopadhyay
The Ohio State University
Columbus OH
kevinm@isotope.com
Charles Mullen
Phoenix NMR LLC
Fort Collins CO
jem210@pitt.edu
Norbert Müller
Johannes Kepler University
Linz Austria
eugene.milshteyn@ucsf.edu
Jean-Pierre Munier
JEOL (EUROPE) SAS
Croissy-Sur-Seine France
mark.milton@takeda.com
Lisa Muñoz
Lewis & Clark College
Portland OR
gina@acornnmr.com
Eric Munson
University of Kentucky
Lexington KY
mishra@mayo.edu
Kimiya Murakami
Asahi Kasei Corporation
Fuji City Japan
tmizuno@jeol.co.jp
Miwa Murakami
Kyoto University
Uzi Japan
Ryota Mizushima
RIKEN Quantitative Biology Center
(QBiC)
Suita Japan
leonard.mueller@ucr.edu
mukhopadhyay.12@osu.edu
cm@phoenixnmr.com
norbert.mueller@mac.com
fourny@jeol.fr
munozl@lclark.edu
eric.munson@uky.edu
murakami.kcg@om.asahi-kasei.co.jp
m-murakami@saci.kyoto-u.ac.jp
ryota.mizushima@riken.jp
Joseph Murphy-Boesch
National Institutes of Health
Bethesda MD
dmmontel@uci.edu
Richard Myer
Communication Power Corp
Hauppauge NY
tkmeldrum@wm.edu
David Montelongo
UC Irvine
Irvine CA
soniac@petrobras.com.br
Tony D Montina
University of Lethbridge
Lethbridge AB Canada
Sonia C Menezes
Petrobras/Cenpes
Rio de Janeiro Brazil
eric.moore2@nih.gov
murphyboeschj@mail.nih.gov
rickm@cpcamps.com
tony.montina@uleth.ca
Page 151
DIRECTORY OF PARTICIPANTS (as of March 31, 2015)
Lokesh N
Indian Institute of Science
Bangalore India
Kosuke Ohgo
Dept of Chemistry, University of Hawaii
Honolulu HI
Brent Paultner
ACD/Labs
Toronto ON Canada
Suryaprakash Nagarajarao
Indian Institute of Science
Bangalore India
Christopher O'Keefe
University of Windsor
Windsor ON Canada
Kari Pederson
University of Georgia
Athens GA
Mahmoud Nasr
Harvard University
Boston MA
Yusuke Okuno
University of Wisconsin-Madison
Madison WI
Istvan Pelczer
Princeton University
Princeton NJ
Nilamoni Nath
Max-Plank Institute for Biophysical Chem
Goettingen Germany
Dean Olson
Univ. of Illinois
Urbana IL
Perry J Pellechia
University of South Carolina
Columbia SC
Gil Navon
Tel Aviv University
Tel Aviv Israel
Stanley Opella
University of California, San Diego
La Jolla CA
Matthew Nethercott
Revolution NMR
Fort Collins CO
Michael Opyr
University of Lethbridge
Lethbridge AB Canada
sopella@ucsd.edu
Chen Peng
Mestrelab Research
Santiago De Compostela A Coruna
Spain
Alexander A. Nevzorov
North Carolina State University
Raleigh NC
Takashi Orikasa
Taiyo Nippon Sanso Corporation
Tokyo Japan
michael.opyr@uleth.ca
Manuel Perez Pacheco
Mestrelab Research
Santiago de Composta Spain
Timothy Newman
UC Davis
Woodland CA
Thomas Osborn Popp
UC Berkeley Jeff Reimer Group
Berkeley CA
Takashi.Orikasa@tn-sanso.co.jp
Robert D. Peterson
UCLA Chemistry and Biochemistry
Los Angeles CA
Bao D. Nguyen
Pfizer, Inc.
Groton CT
Michael Overduin
University of Birmingham
Birmingham UK
tosbornp@berkeley.edu
Ronald Peterson
Daedalus Innovations
Aston PA
Qing Zhe Ni
Massachusetts Institute of Technology
Cambridge MA
Ralph Page
University of California at Berkeley
Castro Valley CA
m.overduin@bham.ac.uk
Francis Picart
Stony Brook University
Stony Brook NY
Walter P. Niemczura
University of Hawaii
Honolulu HI
Arthur G Palmer
Columbia University
New York NY
RalphPage100@yahoo.com
Alex Pines
UC Berkeley
Berkeley CA
Andrew Nieuwkoop
Leibniz Institute Fuer Molekular
Pharmakologie
Berlin Germany
Borlan Pan
Genentech, Inc.
South San Francisco CA
agp6@columbia.edu
Arthur Pinon
EPFL
Lausanne Switzerland
borlanp@gene.com
Guido Pintacuda
CNRS - ENS Lyon
Lyon France
loke.chem@gmail.com
nsp@sif.iisc.ernet.in
mahmoud_nasr@hms.harvard.edu
nnat@nmr.mpibpc.mpg.de
navon@post.tau.ac.il
matthew.nethercott@gmail.com
alex_nevzorov@ncsu.edu
tnewman@ucdavis.edu
bao.nguyen@pfizer.com
qingzhe@mit.edu
walt@hawaii.edu
ohgo@hawaii.edu
okeefe5@uwindsor.ca
okuno@wisc.edu
dolson@illinois.edu
brent.paultner@acdlabs.com
kpederson@ccrc.uga.edu
ipelczer@princeton.edu
pellechia@sc.edu
chen.peng@mestrelab.com
manuel@mestrelab.com
peterson@mbi.ucla.edu
ron@daedalusinnovations.com
Francis.Picart@stonybrook.edu
pines@berkeley.edu
arthur.pinon@epfl.ch
Tadateru Nishikawa
Princess Margaret Cancer Centre, UHN
Toronto ON Canada
Antonios Papaioannou
Graduate Center of
The City University of New York
New York NY
Yusuke Nishiyama
JEOL Ltd.
Tokyo Japan
Rajan K Paranji
University of Washington
Seattle WA
Rostislav Pol
ACD/Labs
Moscow Russia
Maria Luiza Caldas Nogueira
Unicamp
Campinas Brazil
Bu Sik Park
FDA
Silver Spring MD
Tatyana Polenova
University of Delaware
Newark NJ
Rudi Nunlist
Advanced Technology Systems
Kensington CA
Anna Parker
Universiy of California, Berkeley
Berkeley CA
Richard J Porambo
Merck & Co., Inc.
West Point PA
Paul O'Brien
Columbia University
New York NY
Laura B. Pasternack
The Scripps Research Institute
La Jolla CA
Elizabeth Porter
University of North Carolina
Chapel Hill NC
Lauren O’Donnell
University of Miami
Coral Gables FL
Eric K Paulson
Yale University
New Haven CT
Maria Theresia Pöschko
Johannes Kepler University
Linz Austria
nieuwkoop@fmp-berlin.de
tadateru.nishikawa@uhnres.utoronto.ca
yunishiy@jeol.co.jp
marialuiza.nogueira@lnbio.cnpem.br
rudi.nunlist@gmail.com
PennPobe@gmail.com
l.odonnell@umiami.edu
Page 152
apapaioannou@gradcenter.cuny.edu
rajanp@u.washington.edu
bu.park@fda.hhs.gov
ajparker@berkeley.edu
lpastern@scripps.edu
eric.paulson@yale.edu
guido.pintacuda@ens-lyon.fr
Susan Pochapsky
Brandeis University
Waltham MA
ssp@brandeis.edu
pol@acdlabs.ru
tpolenov@mail.chem.udel.edu
rick_porambo@merck.com
porter.elizabeth.anne@gmail.com
maria_theresia.poeschko@jku.at
DIRECTORY OF PARTICIPANTS (as of March 31, 2015)
Alexandra Pozhidaeva
UCONN Health Center
Farmington CT
Todd M Rappe
University of Minnesota
Minneapolis MN
Roland Riek
ETH Zurich
Zurich Switzerland
Sesh Prabhakar
UOP LLC, a Honeywell Company
Des Plaines IL
Ravinder Regatte
NYU Langone Medical Center
New York NY
Chad Rienstra
Univ of Illinois
Urbana IL
Padmanava Pradhan
City University of New York
New York NY
Mikhail Reibarkh
Merck
Rahway NJ
Peter L. Rinaldi
The University of Akron
Akron OH
Subramanian Prasad
BASF Corporation
Iselin NJ
Courtney Reichhardt
Stanford University
Stanford CA
Hattie Ring
University of Minnesota
Minneapolis MN
Carol Preisig
ACD/Labs
Toronto ON Canada
Janice Reid
Tomco Technologies
Stepney Australia
Christopher D. Rithner
Colorado State University
Fort Collins CO
James Prestegard
University of georgia
Athens GA
Bernd Reif
TU Munchen
Garching Germany
Edwin Rivera
University of South Florida
Tampa FL
Marek Pruski
Ames Laboratory, ISU
Ames IA
Michael Reily
Bristol-Myers Squibb
Princeton NJ
Hector Robert
Magritek, USA
San Diego CA
Sergio-Andres Pulido
Karl franzens University-Graz
Graz Austria
Jeffrey Reimer
UC Berkeley
Berkeley CA
Valerie Robertson
University of Guelph
Guelph ON Canada
Zhe Qi
The Ohio State University
Columbus OH
Tony Reinsperger
KIT
Eggenstein-Leopoldshafen Germany
Scott Robson
Harvard Medical School
Boston MA
Feng Qiu
Bristol-Myers Squibb Co.
Pennington NJ
Ewa Rej
University of Sydney
Sydney Australia
Paul Robustelli
D.E. Shaw Research
New York NY
Yun Qu
VCU
Richmond VA
Malin Reller
Karlsruhe Institute of Technology
Karlsruhe Germany
Julien Roche
NIH
Bethesda MD
Mariana Quezado
University of Connecticut Health Center
Farmington CT
Marie Renault
IPBS (UMRCNRS-UPS 5089)
Toulouse France
Chris Roe
DuPont CR&D
Wilmington DE
Daniel Raftery
University of Washington
Seattle WA
William F Reynolds
University of Toronto
Toronto ON Canada
Chris Roe
DuPont CR&D
Wilmington DE
S. Raghothama
Indian Institute of Science
Bangalore India
Anthony A Ribeiro
Duke University
Durham NC
Rivkah Rogawski
Columbia University
New York NY
Paul Ralifo
Boston University
Boston MA
David Rice
Stanford University
Stanford CA
Joseph Romaniuk
Stanford University
Stanford CA
Vijaykumar Ramaswamy
University of Florida
Tallahassee FL
David Richardson
University of Central Florida
Orlando FL
Melanie Rosay
Bruker BioSpin
Billerica MA
Mark Rance
University of Cincinnati
Cincinnati OH
Mark.Rance@UC.Edu
Christian Richter
Ctr for Biomolecular Magnetic
Resonance
Frankfurt Germany
Matthew Rosen
MGH/A.A. Martinos Center
Boston MA
kaili.ranta@gmail.com
Clark D. Ridge
FDA
College Park MD
pozhidaeva@uchc.edu
sesh.prabhakar@uop.com
ppradhan@sci.ccny.cuny.edu
subramanian.prasad@basf.com
carol.preisig@acdlabs.com
jpresteg@uga.edu
mpruski@iastate.edu
sergio.pulido-munoz@uni-graz.at
njuqizhe@gmail.com
feng.qiu@bms.com
yqu@vcu.edu
mariana.quezado@gmail.com
draftery@uw.edu
sr@nrc.iisc.ernet.in
ralifo@bu.edu
r.vijaykumar@ufl.edu
Kaili Ranta
SIUC
Carbondale IL
rapp0006@umn.edu
ravinder.regatte@nyumc.org
mikhail.reibarkh@merck.com
courtney.reichhardt@gmail.com
jreid@tomco.com.au
reif@tum.de
michael.reily@bms.com
reimer@berkeley.edu
tony.reinsperger@kit.edu
erej@physics.usyd.edu.au
malin.reller@kit.edu
marie.renault@ipbs.fr
wreynold@chem.utoronto.ca
anthony.ribeiro@duke.edu
daverice@stanford.edu
david.richardson@ucf.edu
ric@nmr.uni-frankfurt.de
clarkridge@gmail.com
roland.riek@phys.chem.ethz.ch
rienstra@illinois.edu
PeterRinaldi@uakron.edu
hlring@umn.edu
cdr@colostate.edu
edme@usf.edu
hector@magritek.com
vroberts@uoguelph.ca
Scott_Robson@hms.harvard.edu
Paul.Robustelli@DEShawResearch.com
julien.roche@nih.gov
chris.roe@dupont.com
chris.roe@dupont.com
rtrogawski@gmail.com
jaromani@stanford.edu
melanie.rosay@bruker-biospin.com
mrosen@cfa.harvard.edu
Kyle Roskamp
University of California - Irvine
Irvine CA
kroskamp@uci.edu
Page 153
DIRECTORY OF PARTICIPANTS (as of March 31, 2015)
Alfred Ross
Hoffmann LaRoche AG
Basel Switzerland
Kevin Sanders
CNRS
Villeurbanne France
David Schulze Suenninghausen
KIT
Eggenstein-Leopoldshafen Germany
Paolo Rossi
Center for Integrative Proteomics
Research- Rutger
Piscataway NJ
Rahul Sangodkar
University of California Santa Barbara
Santa Barbara CA
Robert W. Schurko
University of Windsor
Windsor ON Canada
prossi@rci.rutgers.edu
Nicolle Sankari
Mount St. Mary's University
Los Angeles CA
Harald Schwalbe
Univ of Frankfurt
Frankfurt Germany
BRoth@som.umaryland.edu
Robert Santorelli
JEOL USA, INC
Peabody MA
Christina Scott
Sigma-Aldrich/Isotec
Miamisburg OH
Gerhard.Roth@bruker.com
Mônica Santos de Freitas
UFRJ
Rio de Janeiro Brazil
Jesse Sears
Battelle PNNL
Richland WA
routak@mail.nih.gov
Muzaddid Sarker
Dalhousie University
Halifax NS Canada
Andrea Sefler
Duke University/Independent
Cary NC
jared.rovny@yale.edu
Mathieu Sarracanie
Dept of Physics, Harvard University
Cambridge MA
Suvrajit Sengupta
University of California, Irvine
Irvine CA
drovnyak@bucknell.edu
Josep Saurí
Merck
Rahway NJ
grace.royappa@stjude.org
Paul Schanda
Institut de Biologie Structurale
Grenoble France
josep.sauri.jimenez@merck.com
Ivan Sergeyev
Columbia Univ / NY Structural Biology
Ctr
New York NY
weiweir0812@gmail.com
paul.schanda@ibs.fr
Herbert Ryan
Bridge12 Technologies, Inc.
Framingham MA
Ulrich Scheler
Leibniz-Institut für Polymerforschung
Dresden e.V.
Dresden Germany
Nikolaos Sgourakis
NIH
Bethesda MD
Joshua Ryan
Magritek Ltd
San Diego CA
Peter Schleker
RWTH Aachen University
Aachen Germany
Hong Shang
UCSF
San Francisco CA
Joseph Sachleben
Univ of Chicago
Chicago IL
Claudia Schmidt
University of Paderborn
Paderborn Germany
Gary Shaw
University of Western Ontario
London ON Canada
Hervé Saint-Jalmes
Centre Eugène Marquis
Rennes France
Sebastian Schmidt
Silantes GmbH
Munich Germany
Roswell Shelhamer
Cambridge Isotope Labs
Tewksbury MA
Chiseko Sakuma
Tokyo Univ of Pharmcy & Life Science
Hachioji Japan
Thomas Schmidt
NIDDK
Rockville MD
Mark Sherwood
IBM Almaden Research Center
San Jose CA
Satoshi Sakurai
JEOL (U.K.) LTD.
Welwyn Garden City UK
Celine Schneider
Memorial University of Newfoundland
St John's NL Canada
Fan Shi
Southern Illinois University
Carbondale IL
Najat Salameh
MGH / Martinos center
Charlestown MA
Thomas Scholz
Dupont CR&D
Wilmington DE
Masahiro Shigezane
Shigemi, Inc.
Allison Park PA
Ago Samoson
NMR Institute
Tallinn Estonia
ago.samoson@gmail.com
Leif Schroeder
Leibniz-Institut fuer Molekulare
Pharmakologie
Berlin Germany
Ichio Shimada
University of Tokyo
Tokyo Japan
et@unc.edu
Patrick Schuenke
German Cancer Research Center
Heidelberg Germany
alfred.ross@roche.com
Braden Roth
University of Maryland, Baltimore
Baltimore MD
Gerhard Roth
Bruker BioSpin GmbH
Karlsruhe Germany
Ashok Rout
National Institutes of Health
Bethesda MD
Jared Rovny
Yale University
Norwalk CT
David Rovnyak
Bucknell University
Lewisburg PA
Grace Royappa
St. Jude Children’s Rsrch Hosp
Memphis TN
WeiWei Ruan
WuHan Inst of Physics and Mathmatics
Wuhan China
herbryan@gmail.com
josh@magritek.com
jsachleben@uchicago.edu
herve.saint-jalmes@univ-rennes1.fr
sakumac@toyaku.ac.jp
satoshi.sakurai@jeoluk.com
najat.salameh@epfl.ch
Ed Samulski
University of North Carolina
Chapel Hill NC
Page 154
kevin.sanders@ens-lyon.fr
rahulsangodkar@umail.ucsb.edu
nicosank@mymsmc.la.edu
santorelli@jeol.com
msfreitas@bioqmed.ufrj.br
muzaddid.sarker@dal.ca
msarraca@physics.harvard.edu
scheler@ipfdd.de
Schleker@itmc.rwth-aachen.de
claudia.schmidt@uni-paderborn.de
sebastian.schmidt@silantes.com
schmidt.nedlitz@hotmail.de
cmschnei@mun.ca
Thomas.h.scholz@dupont.com
lschroeder@fmp-berlin.de
p.schuenke@dkfz.de
david.suenninghausen@kit.edu
rschurko@uwindsor.ca
schwalbe@nmr.uni-frankfurt.de
christina.scott@sial.com
jesse.sears@pnnl.gov
andrea.sefler@gmail.com
suvrajit82@yahoo.com
isergeyev@gmail.com
sgourakisn@mail.nih.gov
Narasimhamurthy Shanaiah
Chemistry, Virginia Tech
Blacksburg VA
nmrns@vt.edu
shanghong@berkeley.edu
gshaw1@uwo.ca
rshelhamer@isotope.com
marksherwood@us.ibm.com
fanshi2010@gmail.com
shigemi-corp@nifty.com
shimada@iw-nmr.f.u-tokyo.ac.jp
Nahoko Shimokawa
JEOL Resonance
Tokyo Japan
nshimoka@jeol.co.jp
DIRECTORY OF PARTICIPANTS (as of March 31, 2015)
Peter Shin
UCSF
San Francisco CA
Ruth Steele
Johnson & Johnson PRD
Spring House PA
Masato Takahashi
RIKEN CLST
Yokohama Japan
Ting Ann Siaw
UC Santa Barbara
Santa Barbara CA
Natalie Stenzoski
SUNY-Stony Brook
Stony Brook NY
Seizo Takahashi
Shigemi, Inc.
Allison Park PA
Ansgar Siemer
University of Southern California
Los Angeles CA
Richard J. Stevens
Stelar s.r.l
Milwaukee WI
Kiyonori Takegoshi
Kyoto University
Kyoto Japan
Bernd Simon
European Molecular Biology Laboratory
Heidelberg Germany
S. Michael Strain
University of Oregon
Eugene OR
C.T. Tan
Isotec/Sigma-Aldrich
Miamisburg OH
Virgil Simplaceanu
Carnegie Mellon University
Pittsburgh PA
David Strand
Protasis
Marlboro MA
Kong Ooi Tan
ETH Zurich
Zurich Switzerland
Andre J Simpson
University of Toronto
Toronto ON Canada
Erik Strandberg
Karlsruhe Inst. of Technology
Karlsruhe Germany
Mitsuru Tashiro
Meisei University
Hino Japan
Jerzy Sitkowski
National Medicines Institute
Warsaw Poland
Madeleine Strickland
NHLBI, NIH
Bethesda MD
Francis Taulelle
KU Leuven
Heverlee Belgium
Tobias Sjolander
UC Berkeley
Berkeley CA
John Stringer
PhoenixNMR
Loveland CO
Reza Tavakoli Dinani
Dept of Physics, Simon Fraser University
Burnaby BC Canada
Clancy Slack
UC Berkeley
Berkeley CA
Jane Strouse
UCLA Dept of Chem. & Biochem
Los Angeles CA
Michael Tayler
UC Berkeley Physics Department
Berkeley CA
Alex I. Smirnov
North Carolina State University
Raleigh NC
Jochem Struppe
Bruker-Biospin
Billerica MA
Ville-Veikko Telkki
University of Oulu
Oulu Finland
Serge Smirnov
Western Washington University
Bellingham WA
Yongchao Su
Merck Research Laboratories
West Point PA
Razvan Teodorescu
Bruker BioSpin Corp.
Billerica MA
Adam Smith
University of Florida
Gainesville FL
Hiroto Suematsu
JEOL Resonance Inc.
Tokyo Japan
Tsutomu Terauchi
Taiyo Nippon Sanso Corporation
Shinagawa-ku Japan
Karen Ann Smith
University of New Mexico
Albuquerque NM
Cheng Sun
Dalian University
Dalian China
Theint Theint
The Ohio State University
Columbus OH
Michael B Smith
Novartis (NIBR)
Cambridge MA
Sandip Sur
U of Rochester
Pittsford NY
Thomas Theis
Duke University
Durham NC
Scott Smith
Tecmag Inc.
Houston TX
Chris Suszczynski
Isotec Stable Isotopes
Miamisburg OH
Thorsten Thiel
Bruker BioSpin
Ettlingen Germany
Nils Spengler
IMT, Karlsruhe Institute of Technology
Eggenstein-Leopoldshafen Germany
Andre Sutrisno
University of Illinois at UrbanaChampaign
Urbana IL
M. Albert Thomas
UCLA School of Medicine
Los Angeles CA
peter.shin@ucsf.edu
siawthony@gmail.com
asiemer@usc.edu
simon@embl.de
vs2a@andrew.cmu.edu
andre.simpson@utoronto.ca
j.sitkowski@nil.gov.pl
tobias_sjolander@berkeley.edu
slackc@berkeley.edu
Alex_Smirnov@ncsu.edu
smirnov@chem.wwu.edu
adams@ufl.edu
karenann@unm.edu
michaelb.smith@novartis.com
ssmith@tecmag.com
nils.spengler@kit.edu
Pavlos Stampoulis
JEOL
pstampou@jeol.co.jp
Ruth E Stark
City University of New York
New York NY
stark@sci.ccny.cuny.edu
Joshua Steele
University of California, Davis
Davis CA
rsteele1@its.jnj.com
natalie.stenzoski@stonybrook.edu
rich.stevens@molspec.com
mstrain@uoregon.edu
d.strand@protasis.com
erik.strandberg@kit.edu
maddy.davison@nih.gov
js@phoenixnmr.com
strousej@chem.ucla.edu
Jochem.Struppe@Bruker-Biospin.com
yongchao.su@merck.com
suematsu@jeol.co.jp
suncheng514@hotmail.com
sandip.sur@gmail.com
chris.suszczynski@sial.com
masatot@gsc.riken.go.jp
takahashi.seizo@gmail.com
takeyan@kuchem.kyoto-u.ac.jp
c.t.tan@sial.com
kota@nmr.phys.chem.ethz.ch
tashiro@chem.meisei-u.ac.jp
francis.taulelle@biw.kuleuven.be
rtavakol@sfu.ca
mcdtayler@berkeley.edu
ville-veikko.telkki@oulu.fi
razvan.teodorescu@bruker.com
terauchi.sail@gmail.com
theint.1@osu.edu
tho.theis@gmail.com
thorsten.thiel@bruker.com
athomas@mednet.ucla.edu
asutrisn@illinois.edu
Kent Thurber
NIH
Bethesda MD
ssweeney@utexas.edu
Fang Tian
Penn State College of Medicine
Hershey PA
Shannon Sweeney
University of Texas at Austin
Austin TX
Brian D. Sykes
University of Alberta
Edmonton AB Canada
brian.sykes@ualberta.ca
thurberk@mail.nih.gov
ftian@psu.edu
jasteele@ucdavis.edu
Page 155
DIRECTORY OF PARTICIPANTS (as of March 31, 2015)
Istvan Timari
University of Debrecen
Debrecen Hungary
Krisztina Varga
University of Wyoming
Laramie WY
Connie Wang
JS Research, Inc.
Quincy MA
Luzineide Tinoco
Federal University of Rio de Janeiro
Rio de Janeiro Brazil
Christophoros Vassiliou
UC Berkeley
Berkeley CA
Hong Wang
Pfizer
Groton CT
Joel R Tolman
Johns Hopkins University
Baltimore MD
S. Sendhil Velan
SBIC
Singapore
Hsin Wang
CUNY - City College
New York NY
Lusine Topchyan
Mount Saint Marys Univ
North Hollywood CA
Santhana Velupillai
University of Iowa/Dept of Chemistry
Iowa City IA
Jin-Shan Wang
JS Research, Inc.
Quincy MA
Yusuho Toyoda
JEOL
Peabody MA
Palamadai Venkatasubramanian
NorthShore Univ. HealthSystem
Evanston IL
Keyu Wang
Gilead
Foster City CA
Nate Traaseth
New York University
New York NY
traaseth@nyu.edu
Stéphane Viel
Aix-Marseille Univ.
& CNRS, ICR UMR 7273
Marseille France
Lei Wang
Hawaii Pacific University
Kaneohe HI
dantraf@comporium.net
Daniel B Vigneron
University of California
San Francisco CA
christoph.trautwein@imtek.uni-freiburg.de
Markus Voehler
Vanderbilt University
Nashville TN
julien.trebosc@univ-lille1.fr
Beat Vogeli
Swiss Federal Institute of Technology,
ETH Zurich
Zürich Switzerland
ront@isotope.com
Thomas Vosegaard
University of Aarhus
Aarhus Denmark
truxal@berkeley.edu
Liliya Vugmeyster
University of Alaska Anchorage
Anchorage AK
yu.tsutsumi@bruker.com
David Waddington
University of Sydney
Sydney Australia
timari.istvan@science.unideb.hu
luzitinoco@hotmail.com
tolman@jhu.edu
lusitopc@mymsmc.la.edu
toyoda@jeol.com
Daniel Traficante
University of RI
Fort Mill SC
Christoph Trautwein
Karlsruhe Institute of Technology
Eggenstein-Leopoldshafen Germany
Julien Trebosc
Université de Lille
UCCS-CNRS UMR8181
Villeneuve d'Ascq Cedex France
Ron Trolard
Cambridge Isotope Labs, Inc.
Tewksbury MA
Ashley Truxal
UC Berkeley
Berkeley CA
Yu Tsutsumi
Bruker Biospin
Yokohama Kanagawa, Japan
Eric Twum
Indiana University
Bloomington IN
ebtwum@indiana.edu
kvarga@uwyo.edu
vassiliou@berkeley.edu
sendhil_velan@sbic.a-star.edu.sg
santhana-velupillai@uiowa.edu
pnvenkat2004@yahoo.com
Tuo Wang
Massachusetts Institute of Technology
Cambridge MA
miao.wang@wilmad-labglass.com
tiawang@utmb.edu
tuowang@mit.edu
beat.voegeli@phys.chem.ethz.ch
Wei Wang
Pfizer
San Diego CA
tv@chem.au.dk
Xiaoling Wang
Department of Chemistry, Virginia Tech
Blacksburg VA
aflv@uaa.alaska.edu
Yanfei Wang
University of Pennsylvania
Philadelphia PA
d.waddington@physics.usyd.edu.au
Yaqiang Wang
University of California Los Angeles
Los Angeles CA
Charles Wade
Los Gatos CA
wei.wang@pfizer.com
mbcocoa@vt.edu
yanfeiw@sas.upenn.edu
yaqiang@mbi.ucla.edu
cwade13@Yahoo.com
Yulan Wang
Wuhan Inst of Phys and Math
Wuhan China
wagner@hms.harvard.edu
Matthias Wapler
University of Freiburg, IMTEK
Freiburg Germany
walder.13@osu.edu
Meaghan Ward
University of Guelph
Guelph ON Canada
tgwalker@wisc.edu
Lisa Warner
National Renewable Energy Lab
Golden CO
jhwalton@ucdavis.edu
Warren S. Warren
Duke University
Durham NC
Thad Walker
Univ. of Wisconsin-Madison
Madison WI
Patrick C.A. van der Wel
University of Pittsburgh
Pittsburgh PA
Jeffrey Walton
University of California, Davis
Davis CA
David Vandervelde
California Inst. of Technology
Pasadena CA
Joshua Wand
Univ of Pennsylvania
Philadelphia PA
Page 156
lwang@hpu.edu
m.voehler@vanderbilt.edu
Mark Van Criekinge
UCSF
San Francisco CA
davidv@caltech.edu
kwang@gilead.com
Tianzhi Wang
University of Texas Medical Branch
Galveston TX
Brennan Walder
The Ohio State University
Columbus OH
pvdwel@pitt.edu
jsresearch@msn.com
dan.vigneron@radiology.ucsf.edu
Jan van Bentum
Radboud University
Nijmegen The Netherlands
mark.vancriekinge@ucsf.edu
hsin.wang@sci.ccny.cuny.edu
Miao Wang
Wilmad-LabGlass
Vineland NJ
Gerhard Wagner
Dept. Biol. Chem. & Mol. Pharmacologie
Boston MA
J.vanbentum@science.ru.nl
hong.wang2@pfizer.com
s.viel@univ-amu.fr
Kathleen Valentine
University of Pennsylvania
Philadelphia PA
valen@mail.med.upenn.edu
info@jsresearch.com
wand@mail.med.upenn.edu
yulan.wang@wipm.ac.cn
wapler@imtek.de
mward01@uoguelph.ca
lisa.warner@nrel.gov
warren.warren@duke.edu
DIRECTORY OF PARTICIPANTS (as of March 31, 2015)
Roderick E. Wasylishen
Department of Chemistry
Edmonton AB Canada
Johannes Windschuh
German Cancer Research Center
Heidelberg Germany
Hongwei Yao
Massachusetts Institute of Technology
Cambridge MA
Shinichi Watanabe
JEOL Ltd.
Tokyo Japan
Jackie Winzeler
ISOTEC/Sigma-Aldrich
Miamisburg OH
Jeffery L Yarger
Arizona State University
Tempe AZ
Jon Webb
MR Resources, Inc.
Fitchburg MA
Daniel Wisniewski
University of Nottingham
Nottingham UK
Shintaru Yazuka
JEOL
Peabody MA
Robert Webb
3M Corporate Research
St. Paul MN
Velencia Witherspoon
UC Berkeley, Chemical Engineering
Yueqi Ye
JEOL
Beijing China
roderick.wasylishen@ualberta.ca
shwatana@jeol.co.jp
jon@mrr.com
johannes.windschuh@dkfz.de
jacqueline.winzeler@sial.com
daniel.wisniewski@nottingham.ac.uk
vjwitherspoon@berkeley.edu
hwyao@mit.edu
jyarger@gmail.com
yazuka@jeol.com
Sebastian Wegner
Bruker BioSpin
Rheinstetten Germany
Christopher Witte
Leibniz-Institut für Molekulare
Pharmakologie
Berlin Germany
Jia Wei
ZKOXFD
Wuhan China
Johannes Wittmann
ETH Zurich
Zurich Switzerland
Jun Yokoyama
Taiyo Nippon Sanso Corporation
Tsukuba Ibaraki, Japan
Xuan Wei
MIT
Cambridge MA
Klaus Woelk
Missouri S&T
Rolla MO
Robert Young
University of California
Riverside CA
Ruediger Weisemann
Bruker Biospin GmbH
Rheinstetten Germany
Rudy Wojtecki
IBM Almaden Research Center
San Jose CA
Liping Yu
University of Iowa
Iowa City IA
Ulrike Werner-Zwanziger
University of California
Santa Barbara CA
Kurt Wollenberg
Lubrizol Corporation
Wickliffe OH
Yue Yuan
University of Notre Dame
Notre Dame IN
Patrick Wheeler
ACD Labs
Toronto ON Canada
Tricia Wong
UC Davis
Davis CA
Milan Zachrdla
Masaryk University, CEITEC
Brno Czech Republic
Sungsool Wi
NHMFL
Tallahassee FL
Bing Wu
Dublin City University
Dublin Ireland
Moritz Zaiss
German Cancer Research Center
Heidelberg Germany
Jason Widegren
NIST
Boulder CO
CHIN H. WU
University of California, San Diego
La Jolla CA
Jaroslav Zajicek
University of Notre Dame
Notre Dame IN
Scarlett Widgeon
UC Santa Barbara
Santa Barbara CA
Shaoxiong Wu
Emory University
Atlanta GA
Matthew Zambrello
University of Connecticut
Farmington CT
Katherine Wildman
Washington University
Saint Louis MO
Jun Xu
UC Berkeley
El Cerrito CA
Klaus Zangger
University of Graz
Graz Austria
Jonathan Williams
Massachusetts Institute of Technology
Cambridge MA
Qiuwei Xu
Merck Research Laboratories
West Point PA
Tim Zeiske
Columbia University
New York NY
Matthew Willmering
Washington University in STL
St. Louis MO
Liang Xue
Novartis Company
Fort Worth TX
Toby Zens
JEOL USA
Peabody MA
Donald Wilson
Retired
Berkeley CA
Zhimin Yan
National Institute for Nanotechnology
Edmonton AB Canada
Jianping Zhang
Bruker BioSpin Corp
Beijing China
Stephen Wimperis
University of Glasgow
Glasgow UK
Hao Yang
Chem. Dept., Washington Univ.
St. Louis MO
Le Zhang
UNC Chapel Hill
Chapel Hill NC
rjwebb7@mmm.com
sebastian.wegner@bruker.com
jay.wei@outlook.com
xuanw@mit.edu
ruediger.weisemann@bruker.com
ulli.zwanziger@Dal.ca
patrick.wheeler@acdlabs.com
sungsool@magnet.fsu.edu
jason.widegren@nist.gov
swidgeon@engineering.ucsb.edu
khenzler@gmail.com
jkw13@mit.edu
mwillmering@wustl.edu
windansea@sprintmail.com
s.wimperis@chem.gla.ac.uk
chris@witte.net.au
jowi@nmr.phys.chem.ethz.ch
woelk@mst.edu
rjwojtec@us.ibm.com
kfw@lubrizol.com
trcwong@ucdavis.edu
bing.wu2@mail.dcu.ie
chinwu@ucsd.edu
swu@emory.edu
qidongxujun@gmail.com
qiuwei_xu@merck.com
liang.xue@alcon.com
zhimin.yan@nrc.ca
hyang@go.wustl.edu
ye.yueqi@jeol.com.cn
Jiewen Ying
Sigma-Aldrich Co
Germantown WI
jiewen.ying@sial.com
Jun.Yokoyama@tn-sanso.co.jp
ryoun003@ucr.edu
Liping-yu@uiowa.edu
yyuan1@nd.edu
324489@mail.muni.cz
m.zaiss@dkfz.de
jzajicek@nd.edu
zambrello@uchc.edu
klaus.zangger@uni-graz.at
tz2155@cumc.columbia.edu
toby.zens@sbcglobal.net
jianping.zhang@bruker.com
lez@unc.edu
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DIRECTORY OF PARTICIPANTS (as of March 31, 2015)
Meng Zhang
University of Michigan
Ann Arbor MI
New York University
Jersey city NJ
yz954@nyu.edu
College of Staten Island
City University of New York
Staten Island NY
zmzt@umich.edu
Zhenchao Zhao
Xiamen University
Xiamen China
rozhang@umich.edu
Jianping Zhong
Wuhan Inst of Physics and Mathematics
Wuhan China
weixing.zhang@stjude.org
Ronghui Zhou
Colgate-Palmolive Company
Piscataway NJ
xiaolu.zhang@novartis.com
Yong Zhang
Stevens Institute of Technology
Hoboken NJ
Xin Zhou
Wuhan Inst of Physics &
Mathematics/CAS
Wuhan Hubei, China
Yongbo Zhang
Northwestern University
Evanston IL
Zhe Zhou
The Dow Chemical Company
Freeport TX
Nicholas Zumbulyadis
Eastman Kodak (retired)
Rochester NY
Yonghong Zhang
Univ. of Texas-Pan American
Edinburg TX
Zijian Zhou
Duke University
Durham NC
Niels Zussblatt
University of California, Santa Barbara
Santa Barbara CA
Yuning Zhang
Jianqin Zhuang
Rongchun Zhang
the University of Michigan
Ann Arbor MI
Weixing Zhang
St. Jude Children's Research Hospital
Memphis TN
Xiaolu Zhang
Novartis
Cambridge MA
yong.zhang@stevens.edu
ybzhang@northwestern.edu
zhangy@utpa.edu
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jianqin.zhuang@csi.cuny.edu
Zhenchao.Zhao@pnnl.gov
Joshua Ziarek
Harvard Medical School
Boston MA
zhongjianpingwuli@126.com
Fabio Ziarelli
Aix-Marseille Univ.CNRS
Marseille France
zhou.uf@gmail.com
John S. Zintsmaster
Chevron Energy Tech. Co.
Richmond CA
xinzhou@wipm.ac.cn
zzhou@dow.com
zz38@duke.edu
jjziarek@gmail.com
fabio.ziarelli@univ-amu.fr
JZintsmaster@chevron.com
Erik Zuiderweg
University of Michigan Medical School
Ann Arbor MI
zuiderwe@umich.edu
nickz@frontiernet.net
niels_p_zussblatt@umail.ucsb.edu
MEMORIAL
ENC remembers three people who are well-known to our community and will be greatly missed.
John S. Waugh, an MIT Professor emeritus died Friday, Aug. 22, 2014 at the age of 85.
Waugh was an authority in chemical physics, known internationally for his work in
magnetic resonance.
“His contribution was the discovery of an entire field of research that enables
science to elucidate structures of molecules and very small particles without breaking
them or crushing them,” said Oded Gonen, a former colleague, New York University
School of Medicine.
"He basically invented the field of solid-state NMR when everyone else had left
the field because they thought it was never going to work. There are a huge number of
people working in it, and it's all because of things that happened in John Waugh's lab.
He made some incredible innovations that have led to many important scientific steps
forward, and today solid-state NMR is a vibrant enterprise," says Robert Griffin, an MIT
professor of chemistry who was a postdoc in Waugh's lab in the 1970s.
“NMR is not so much a field of science, bent on the study and understanding of
nature, as it is a collection of tools that can be used in studying such fields,” John
Waugh wrote in an autobiographical essay. “As such, it is advanced by invention more
than by the discovery of new concepts. I have found that in inventing new tools for
chemists and biologists, I have learned parts of physics and mathematics that I would
not have had the pleasure of studying otherwise. In any case, I have been content to
find and exhibit new tricks, for the most part leaving it to others to apply them to their own specialties.”
Excepted from The Boston Globe, October 19, 2014.
Woody W. Conover
1947 - 2014
Woody was born in Terre Haute, IN. His father was a bricklayer, and Woody
put himself through college working summers as a bricklayer. He was a HAM radio
operator growing up, and his resulting understanding of RF electronics became a
component of his interest in NMR. He earned a B.S. in Chemistry, Rose Hulman
Polytechnic Institute, 1969, and a Ph.D. in synthetic organic chemistry, Indiana
University, 1973. After a post-doc at University of Chicago working on NMR of
prostaglandins, he became an adjunct professor and Operations Manager of the
Stanford NMR Lab at Stanford University.
In 1978, he joined Nicolet Technology. In 1981, Nicolet wanted a functioning
spectrometer in the suite at ENC, which wasn’t possible because vendors could not
access suites until Sunday. The solution? They loaded an energized 500 magnet on a
truck and drove it from Mt. View, CA to Asilomar. The magnet survived the trip at field!
In 1982, Woody proposed and headed a project to create an inexpensive
automated routine NMR spectrometer; and the QE-300 was born. In 1983, Woody became manager of engineering for GE NMR
Instruments. In 1988, he co-founded Fremont Magnetic Resonance, providing NMR probes and consulting services. Acorn NMR
was started in 1991 to provide NMR spectroscopy services to other companies. He ventured into programming, with the goal of
creating PC-based NMR data processing software, which became the NUTS program.
Woody served on the ENC Executive Committee twice, and could be found at every ENC hosting a vendor suite. He
was also instrumental in establishing wine tasting during the Asilomar ENC poster sessions. Outside of work, Woody applied his
chemistry training to cooking and amateur wine making.
Allison Lin
January 23, 2015
Allison succumbed to liver cancer at the age of 67. She started attending ENC over 20 years ago with
Shigemi Inc. and quickly became a fixture of the conference. She not only helped make a significant
contribution to NMR research but also became a constant that all attendees remember. Everyone
always looked forward to stopping by Shigemi for sushi and a warm smile from the “Shigemi Lady.” She
was an extraordinary and kind person who loved her ENC friends and made each of us feel special
when she greeted and remembered so many of us.
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