Michael S.
Chimenti
PhD
“Michael has been the linchpin
in our protein-targeted drug
discovery
project[…]he
is
exceptionally versatile and his
communication skills enable
him to sync well with other
researchers possessing varied
backgrounds. […]”
-Tom James, PhD
Professor and Chair Emeritus,
Dept of Pharmaceutical
Chemistry, UCSF
“Michael has a number of key
strengths that will make him
an asset to team-based
research in a pharmaceutical
or biotechnology environment.”
-Matt Jacobson, PhD
Professor and Vice Chair, Dept
of Pharmaceutical Chemistry,
UCSF
“Michael is an extremely
competitive candidate…he is
smart and highly motivated”
-Torsten Wittman, PhD
Prof, Dept of Tissue and Cell
Biology
PROFILE
PhD scientist with expertise in structural biology and biophysics, computational chemistry,
drug discovery, fragment screening, data science, and technical writing
SPECIAL SKILLS
Execution – regularly delivering critical data on time and within budget
Collaboration – 3 years experience on top-ranked NCI drug development team
Communication – First-author papers in top journals, Nature review, popular blog
RELEVANT COURSEWORK
Python for Scientists and Engineers (Enthought 5-day workshop)
--covered iPython, NumPy, SciPy, Pandas, Cython, and Traits
R Programming (Johns Hopkins Online)
Getting and Cleaning Data (Johns Hopkins Online)
Exploratory Data Analysis (Johns Hopkins Online)
2014
2014
2014
2014
EDUCATION
Postdoctoral Scholar, University of California, San Francisco
Department of Pharmaceutical Chemistry
2009 - present
Biophysics, PhD, The Johns Hopkins University, Baltimore, MD.
2003-2009
Biochemistry, BSc with Honors, University of Iowa, Iowa City, IA.
1999-2003
RESEARCH
Development of high affinity drug leads with NMR and computational modeling 2014
Fragment-based drug discovery screening using biophysical methods against p97 2013




Discovered 15 specific, good affinity fragment “hits” to p97 using NMR
Guided hit-to-lead efforts using computational modeling tools
Our p97 team project is top-rated by the National Cancer Institute
Acquired cutting-edge NMR spectra of the extremely large p97 hexamer bound to a variety
of ligands including ADP, ATP and fragment “hits”
Computational prediction of pH regulation of FAK-FERM Kinase
2012
Determined novel ‘molecular Velcro’ binding mode of intrinsically disordered CLASP2
with EB1 microtubule associating protein
2010
michael.chimenti@gmail
.com
(410)-271-9415 (cell)



Predicted a novel hyper-phosphorylated regulatory mechanism in CLASP2 using explicit
solvent molecular dynamics and other computational tools
Demonstrated the correctness of computational predictions by designing and carrying out
fluorescence polarization assays of wtCLASP2 and mutants to measure affinities for EB1
Supported predicted intra-molecular interactions in CLASP2 by 31P NMR of custom peptides
PhD: Examined the determinants of pKa values of internal ionizable groups in proteins
Visit my website for
examples of my technical
writing and coding skills:
michaelchimenti.com



Performed a large systematic biophysical study of the dielectric response of proteins
Provided the first comprehensive experimental dataset on protein dielectric response to
charging an internal ionizable group
My dataset was used to guide computational model development by others in the field
PUBLICATIONS
Chimenti MS, Bulfer S, Tjhen R, Kelly MS, Jacobson MP, Arkin M (2014). Fragment-based
drug discovery against a p97/VCP ATPase. Accepted for publication at the Journal of
Biomolecular Screening.
Chimenti MS, Kumar P, Pemble H, Thompson O, Jacobson MP, and Wittmann T (2012).
Multisite phosphorylation modulates CLASP-EB1 interactions by disrupting arginineglutamate salt bridge networks. Journal of Biological Chemistry. 287: 17050-17064. ‘Faculty
of 1000’ Awarded for Special Significance in the Field
Chimenti MS, Khangulov VS, Robinson AC, Heroux A, Majumdar A, Schlessman JL and
Garcia-Moreno B (2012). Structural reorganization coupled to the ionization of internal
residues in proteins; survey of 25 lysine residues. Structure. 20 (6): 1071-1085.
Chimenti MS, Castaneda CA, Majumdar A, Garcia-Moreno B (2011). Structural origins of
high apparent dielectric constants experienced by ionizable groups in the hydrophobic core
of a protein. Journal of Molecular Biology. 405 (2): 361-377.
Choi, C, Webb BA, Chimenti MS, Jacobson MP, and Barber DL (2013). pH Sensing by FAKHis58 Regulates Focal Adhesion Remodeling. Journal of Cell Biology. 202 (6): 849-859.
‘Faculty of 1000’ Awarded for Special Significance in the Field
Pfaff SJ, Chimenti MS, Kelly MJS, and Arkin MR (2013). Biophysical methods for identifying
fragment-based inhibitors of protein-protein interactions. Methods in Molecular Biology.
[Book Chapter].
Webb BA, Chimenti MS, Jacobson MP, and Barber DL (2011). Dysregulated pH: A Perfect
Storm for Cancer Progression. Nature Reviews Cancer 11: 671-677.
Baran KL, Chimenti MS, Schlessman JL, Fitch CA, Herbst KJ, and Garcia-Moreno B (2008).
Electrostatic effects in a network of polar and ionizable groups in staphylococcal nuclease.
Journal of Molecular Biology 379: 1045-1062.
Harms MJ, Schlessman JL, Chimenti MS, Sue GR, Damjanovic A, and Garcia-Moreno B
(2008). A buried lysine that titrates with a normal pKa: Role of conformational flexibility at
the protein water interface as a determinant of pKa values. Protein Science 17: 833-845.
Takayama Y, Castaneda CA, Chimenti MS, Garcia-Moreno B, and Iwahara J (2008). Direct
Evidence for Deprotonation of a Lysine Side Chain Buried in the Hydrophobic Core of a
Protein. Journal of the American Chemical Society 130: 6714-6715.
Schroer MS, Paulus M, Jeworrek C, Krywka C, Schmacke S, Zhai Y, Chimenti MS, Royer, CA,
Garcia-Moreno B, Toland M, and Winter R (2010). High Pressure SAXS study of folded and
unfolded ensembles of a protein. Biophysical Journal 99 (10): 3430-3437.
Kitahara R, Hata K, Maeno A, Akasaka K, Chimenti MS, Garcia-Moreno B, Schroer MA,
Jeworrek C, Toland M, Winter R, Roche J, Roumestand C, Montet de Guillen K, and Royer AC
(2011). Structural plasticity of staphylococcal nuclease probed by perturbation with
pressure and pH. Proteins 79 (4): 1293-1305.