Curriculum vitae
ROBERT LESH BALDWIN
EDUCATION
University of Wisconsin, B.A., 1950, Chemistry
Oxford University, England, D.Phil., 1954, Biochemistry (with A.G. Ogston)
University of Wisconsin, 1954–55, Postdoctoral training: Physical Chemistry (with J.W. Williams and
L.J. Gosting).
RESEARCH AND PROFESSIONAL EXPERIENCE
1955–1959
University of Wisconsin (Madison), Department of Biochemistry
Assistant Professor 1955–1958; Associate Professor 1958–1959
1959–Present
Stanford University, Department of Biochemistry: Associate Professor 1959–1964;
Professor 1964–1998; Chairman 1989–1994; Professor Emeritus 11/1/98–present
1958–1959
Research leave: (8 months), Carlsberg Laboratory (section of K. Linderstrøm–Lang),
Copenhagen
1961
Research leave (3 months) National Institutes of Health, with David Davies
1963–1964
Research leave (3 months) Max Planck Institut für physikalische Chemie (section of
M. Eigen), Göttingen; 9 months, Institut Pasteur (sections of F. Jacob and J. Monod),
Paris
1971–1972
Sabbatical leave, Institut Pasteur, Départment Biologie Moléculaire (section of F.
Jacob), Paris
1978–1979
Sabbatical leave, MRC Laboratory of Molecular Biology (Structural Studies Division)
Cambridge, England
HONORS AND SERVICE
1950–1953
Rhodes Scholar
1958–1959
Guggenheim Fellow
1963–1964
NIH Senior Fellow
1964–68, 75–79 Member of Editorial Board, Journal of Molecular Biology
1969–1971
USPHS Fellowship Committee, Biochemistry and Molecular Biology
1974–1976
NSF Advisory Panel, Biochemistry and Biophysics
1977–1984
Editorial Board, Trends in Biochemical Science
1977–1981
Council, Biophysical Society of America
1980–Present
Member, U.S. National Academy of Sciences
1981–Present
Member, American Academy of Arts and Sciences
1982
Member, Oversight Panel for the Section of Molecular and Genetic Biosciences,
National Science Foundation
1984–2008
Editorial Advisory Board, Biochemistry
1984–1988
Panel Member, NIH Study Section on Molecular and Cellular Biophysics
1986
1986–Present
1988
1989
1992–1997
1992
1993–1996
1993–1995
1993
1994
1995
1996–2001
1996
1999
1999
2000
Member of National Academy of Sciences Research Briefing Panel on Protein
Structure and Biological Function
Member, Editorial Board, Proteins
NIH Merit award
Member, Visiting Committee for the Biological Sciences, Rice University
Member, Editorial Advisory Board, Protein Science
Stein & Moore Award of the Protein Society
Searle Scholars Advisory Committee
Council of the Protein Society
Member, Visiting Committee for Biochemistry and Molecular Biology
Rutgers University
Research Fellow of the Japanese Society for the Promotion of Science
Wheland Award in Chemistry, University of Chicago
Advisory Committee, Burroughs Wellcome Interface Program
Member, External Review Committee, University of Colorado Department of
Molecular, Cellular and Developmental Biology
Founder's Award, Biophysical Society
Merck Award, American Society for Biochemistry and Molecular Biology
Fellow, Biophysical Society
LECTURES
1972
1986
1987
1988
1988
1990
1991
1993
1993
1996
1997
1998
2002
Visiting Professor, Collège de France, Paris
Leach Lecture, Lorne, Australia
Hutchison Lectures, University of Rochester
Alpha Chi Sigma Lecture, University of Illinois
Oncley Lecture, University of Michigan
Foster Lecture, Purdue
Plenary Lecture at Keystone Meeting on "Protein Folding, Structure and Function"
Keynote address, Howard Hughes Meeting on Macromolecular Assembly
Everson Lecture, University of Wisconsin
Keynote Address, Texas Protein Folders meeting
Anfinsen Lecture, Johns Hopkins Folding Meeting
Willard Lectures, University of Wisconsin
University Lecture, Tsinghua University, Beijing
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PUBLICATIONS
1950 R.L. Baldwin and J.W. Williams, "Boundary Spreading in Sedimentation Velocity Experiments."
J. Am. Chem. Soc. 72, 4325.
1951 R.A. Alberty and R.L. Baldwin, "A Mathematical Theory of Immune Hemolysis." J. Immunol. 66,
725-735.
1951 R.L. Baldwin, P.M. Laughton and R.A. Alberty, "Homogeneity and the Electrophoretic Behavior
of Some Proteins. III A General Method for the Determination of Mobility Distributions." J. Phys.
Colloid Chem. 55, 111-125.
1952 J.W. Williams, R.L. Baldwin, W.M. Saunders and P.G. Squire, "Boundary Spreading in
Sedimentation Velocity Experiments. I. The Enzymatic Degradation of Serum Globulins." J. Am.
Chem. Soc. 74, 1542-1552.
1953 R.L. Baldwin, "Sedimentation Coefficients of Small Molecules: Methods of Measurement Based
on the Refractive-Index Gradient Curve. The Sedimentation Coefficient of Polyglucose A."
Biochem. J. 55, 644-648.
1953 R.L. Baldwin "The Neurotoxin of Shigella Shigae. 2. Examination of the Toxin in the Oil-turbine
Ultracentrifuge." B. J. Exp. Path. 34, 217-220.
1954 R.L. Baldwin, "Boundary Spreading in Sedimentation Velocity Experiments. II. The Correction of
Sedimentation Coefficient Distributions for the Dependence of Sedimentation Coefficient on
Concentration." J. Am. Chem. Soc. 76, 402-407.
1954 R.L. Baldwin, "Boundary Spreading in Sedimentation Velocity Experiments. III. Effects of
Diffusion on the Measurement of Heterogeneity when Concentration Dependence Is Absent."
J. Phys. Chem. 58, 1081-1086.
1954 R. L. Baldwin and A.G. Ogston, "The Diffusion and Sedimentation Coefficients of a Liquid Twocomponent System in Terms of Macroscopic Properties of the System." Trans. Faraday Soc. 50,
749-755.
1955 R.L. Baldwin, L.J .Gosting, J.W. Williams and R.A. Alberty." "Transport Processes and the
Heterogeneity of Proteins." Faraday Soc. Discussion 20, 13-24.
1955 R.L. Baldwin, P.J. Dunlop and L.J. Gosting, "Interacting Flows in Liquid Diffusion: Equations for
the Evaluation of Diffusion Coefficients from Moments of the Refractive Index Gradient Curves."
J. Am. Chem. Soc. 77, 5235-5238.
1957 R.L. Baldwin, "Boundary Spreading in Sedimentation Velocity Experiments. 4. Measurement of
the Standard Deviation of a Sedimentation Coefficient Distribution: Application to Bovine
Albumin and -Lactoglobulin." Biochem. J. 65, 490-502.
1957 R.L. Baldwin, "Boundary Spreading in Sedimentation Velocity Experiments. 5. Measurement of
the Diffusion Coefficient of Bovine Albumin by Fujita's Equation." Biochem. J. 65, 503-512.
1958 K.E. Van Holde and R.L. Baldwin, "Rapid Attainment of Sedimentation Equilibrium." J. Phys.
Chem. 62, 734-743.
1958 R.L. Baldwin, "Molecular Weights from Studies of Sedimentation and Diffusion in ThreeComponent Systems." J. Am. Chem. Soc. 80, 496.
1958 R.Y.H. Hsu, L. Anderson, R.L. Baldwin, C.A. Ernstrom and A.M. Swanson, "Rennin Coagulation
of Enzymatically Dephosphorylated Casein." Nature 182, 798-799.
1958 J.W. Williams, K.E. Van Holde, R.L. Baldwin and H. Fujita, "The Theory of Sedimentation
Analysis." Chem. Rev. 58, 715-806.
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1958 I.J. O'Donnell, R.L. Baldwin and J.W. Williams, "Correlation of the N
Thyroglobulin with the Type of Breakdown Produced by Papain." Biochim. Biophys. Acta 28, 294308.
1959 R.L. Baldwin, "Equilibrium Sedimentation in a Density Gradient of Materials having a
Continuous Distribution of Effective Densities." Proc. Natl. Acad. Sci. USA 45, 939-944.
1959 R.L. Baldwin, "Boundary Spreading in Sedimentation Velocity Experiments. VI. A Better Method
for Finding Distributions of Sedimentation Coefficient when the Effects of Diffusion are Large."
J. Phys. Chem. 63, 1579-1573.
1960 R.L. Baldwin and K.E. Van Holde, "Sedimentation of High Polymers." Fortschr. Hochpolym.Forsch. 1, 451-511.
1960 J.G. Kirkwood, R.L. Baldwin, P.J. Dunlop, L.J. Gosting and G. Kegeles, "Flow Equations and
Frames of Reference for Isothermal Diffusion in Liquids." J. Chem. Phys. 33, 1505-1513.
1961 R.G. Wake and R.L. Baldwin, "Analysis of Casein Fractions by Zone Electrophoresis in
Concentrated Urea." Biochim. Biophys. Acta 47, 225-239.
1962 R.B. Inman and R.L. Baldwin, "Helix–Random Coil Transitions in Synthetic DNA's of
Alternating Sequence." J. Mol. Biol. 5, 172–184.
1962 R.B. Inman and R.L. Baldwin, "Formation of Hybrid Molecules from Two Alternating DNA
Copolymers." J. Mol. Biol. 5, 185–200.
1962 R.G. Wake and R.L. Baldwin, "Physical Studies on the Replication of DNA in vitro." J. Mol.
Biol. 5, 201–216.
1962 A.D. Kaiser and R.L. Baldwin, "A Relation between Dinucleotide and Base Frequencies in
Bacterial DNAs." J. Mol. Biol. 4, 418-419.
1962 F.E. LaBar and R.L. Baldwin, “A Study By Interference Optics of Sedimentation in Short
Columns." J. Phys. Chem. 66, 1952-1957.
1963 F.E. LaBar and R.L. Baldwin, "The Sedimentation Coefficient of Sucrose." J. Am. Chem. Soc. 85,
3105-3108.
1963 R.L. Baldwin, "Thermodynamic Properties of Proteins Found from Osmotic Experiments" in
Comprehensive Biochemistry Vol. 7, ed. by M. Florkin and E.H. Stotz, Elsevier, pp. 184-199.
1963 R.L. Baldwin and E.M. Shooter, "Measurement of Density Heterogeneity by Sedimentation in
Preformed Gradients." in Conference on the Ultracentrifuge, ed. by J. W. Williams, Academic
Press, pp. 143–168.
1963 M. Chamberlin, R.L. Baldwin, and P. Berg, "An Enzymically Synthesized RNA of Alternating
Base Sequence: Physical and Chemical Characterization." J. Mol. Biol. 7, 334–349.
1963 D.R. Davies and R.L. Baldwin, "X–ray Studies of Two Synthetic DNA Copolymers." J. Mol.
Biol. 6, 251–255.
1963 E.M. Shooter and R.L. Baldwin, "The Alkaline Transition of BU–containing DNA and its Bearing
on the Replication of DNA." J. Mol. Biol. 7, 511–526.
1964 T. Kotaka and R.L. Baldwin, "Effects of Nitrous Acid on the dAT Copolymer as a Template for
DNA Polymerase." J. Mol. Biol. 9, 323–339.
1964 R.B. Inman and R.L. Baldwin, "Helix–Random Coil Transitions in DNA Homopolymer Pairs."
J. Mol. Biol. 8, 452–469.
1964 R.L. Baldwin, "Molecular Aspects of the Gene: Replication Mechanisms." in The Bacteria, Vol.
5, ed. by R. Stanier and I.C. Gunsalus, Academic Press, Inc., pp. 327–372.
1965 H.C. Spatz and R.L. Baldwin, "Study of the Folding of the dAT Copolymer by Kinetic
Measurements of Melting." J. Mol. Biol. 11, 213–222.
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1966 M.E. Goldberg, T.E. Creighton, R.L. Baldwin and C. Yanofsky, "Subunit Structure of the
Tryptophan Synthetase of Escherichia coli." J. Mol. Biol. 21, 71–82.
1966 R.L. Baldwin, P. Barrand, A. Fritsch, D.A. Goldthwait and F. Jacob, "Cohesive Sites on the
Deoxyribonucleic Acids from Several Temperate Coliphages." J. Mol. Biol. 17, 343–357.
1967 M.E. Goldberg and R.L. Baldwin, "Interactions between the Subunits of the Tryptophan
Synthetase of Escherichia coli. Optical Properties of an Intermediate Bound to the 2 2
Complex." Biochemistry 6, 2113-2119.
1968 R.L. Baldwin, "Kinetics of Helix Formation and Slippage of the dAT Copolymer," in Molecular
Associations in Biology, ed. by B. Pullman, Academic Press, Inc., pp. 145–162.
1968 J.B. LePecq and R.L. Baldwin, "T
Cold Spring Harbor Symposia on Quantitative Biology, Vol. XXXIII, pp. 609–620.
1968 I.E. Scheffler, E.L. Elson, and R.L. Baldwin, "Helix Formation by dAT Oligomers. I. Hairpin and
Straight–chain Helices." J. Mol. Biol. 36, 291–304.
1969 T. Kotaka and R.L. Baldwin, "Theory of a Rapid Method for Determining Molecular Weights of
Giant Molecules." Biopolymers 7, 87–97.
1970 I.E. Scheffler, E.L. Elson, and R.L. Baldwin, "Helix Formation by d(TA) Oligomers. II. Analysis
of the Helix–Coil Transitions of Linear and Circular Oligomers." J. Mol. Biol. 48, 145–171.
1970 E.L. Elson, I.E. Scheffler, and R.L. Baldwin, "Helix Formation by d(TA) Oligomers.
III. Electrostatic Effects." J. Mol. Biol. 54, 401–415.
1971 T.Y. Tsong, R.L. Baldwin, and E.L. Elson, "The Sequential Unfolding of Ribonuclease A:
Detection of a Fast Initial Phase in the Kinetics of Unfolding." Proc. Natl. Acad. Sci. USA 68,
2712–2715.
1971 R.L. Baldwin, "Experimental Tests of the Theory of Deoxyribonucleic Acid Melting with d(T–A)
Oligomers. Accounts Chem. Res. 4, 265–272.
1971 A.J.D. Bellett, H.G. Busse, and R.L. Baldwin, “Tandem Genetic Duplications in a Derivative of
Phage Lambda.” In The Bacteriophage Lambda, Cold Spring Harbor Lab, New York, pp. 501513.
1972 R.C. Costello and R.L. Baldwin, "The Net Hydration of Phage Lambda." Biopolymers 11, 2147–
2169.
1972 R.C. Costello and R.L. Baldwin, "New Banding Species, with Densities of Phage–Ghost Clusters,
Produced from Lambda Phage Particles on Storage." Biopolymers 11, 2171–2177.
1972 T.Y. Tsong, R.L. Baldwin, and E.L. Elson, "Properties of the Refolding and Unfolding Reactions
of Ribonuclease A." Proc. Natl. Acad. Sci. USA 69, 1809–1812.
l972 T.Y. Tsong and R.L. Baldwin, "Kinetic Evidence for Intermediate States in the Unfolding of
Chymotrypsinogen A." J. Mol. Biol. 69, 145–148.
1972 T.Y. Tsong and R.L. Baldwin, "Kinetic Evidence for Intermediate States in the Unfolding of
Ribonuclease A. II. Kinetics of Exposure to Solvent of a Specific Dinitrophenyl Group." J. Mol.
Biol. 69, 149–153.
1972 H.G. Busse and R.L. Baldwin, "Tandem Genetic Duplications in a Derivative of Phage Lambda.
II. Evidence for Structure and Location of Endpoints." J. Mol. Biol. 65, 401–412.
1972 T.Y. Tsong, R.L. Baldwin, and P. McPhie, "A Sequential Model of Nucleation–Dependent
Protein Folding: Kinetic Studies of Ribonuclease A." J. Mol. Biol. 63, 453–475.
1973 J.–R. Garel and R.L. Baldwin, "Both the Fast and Slow Refolding Reactions of Ribonuclease A
Yield Native Enzyme." Proc. Natl. Acad. Sci. USA 70, 3347–3351.
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1975 J.–R. Garel and R.L. Baldwin, "The Heat–Unfolded State of Ribonuclease A is an Equilibrium
Mixture of Fast and Slow Refolding Species." J. Mol. Biol. 94, 611–620.
1975 J.–R. Garel and R.L. Baldwin, "A Physical Difference Between the Fast– and Slow–refolding
Forms of Nitrotyrosyl Ribonuclease A: the pK Values of the Nitrotyrosyl Groups." J. Mol. Biol.
94, 621–632.
1975 S.W. Emmons, V. MacCosham, and R.L. Baldwin, "Tandem Genetic Duplications in Phage
Lambda. III. The Frequency of Duplication Mutants in Two Derivatives of Phage Lambda is
Independent of Known Recombination Systems." J. Mol. Biol. 91, 133–146.
1975 S.W. Emmons, V. MacCosham and R.L. Baldwin, “On the Mechanism of Production of Tandem
Genetic duplications in Phage Lambda.” J. Mol. Biol. 95, 83-89.
1975 R.L. Baldwin, "Intermediates in Protein Folding Reactions and the Mechanism of Protein
Folding." Ann. Review of Biochem., Vol. 44, pp. 453–475.
1976 P.J. Hagerman and R.L. Baldwin, "A Quantitative Treatment of the Kinetics of the Folding
Transition of Ribonuclease A." Biochemistry 15, 1462–1473.
1976 J.–R. Garel, B.T. Nall, and R.L. Baldwin, "Guanidine–unfolded state of ribonuclease A contains
both fast– and slow–refolding species." Proc. Natl. Acad. Sci. USA 73, 1853–1857.
1976 A.A. Schreier and R.L. Baldwin, "Concentration–dependent Hydrogen Exchange Kinetics of 3H–
labeled S–Peptide in Ribonuclease S." J. Mol. Biol. 105, 409–426.
1977 B.T. Nall and R.L. Baldwin, "Thermal Unfolding Transition of Ribonuclease A Measured by 2'–
CMP Binding." Biochemistry 16, 3572–3576.
1977 C. Christiansen and R.L. Baldwin, "Catalysis of DNA Reassociation by the Escherichia coli DNA
Binding Protein: A Polyamine–dependent Reaction." J. Mol. Biol. 115, 441–454.
1977 A.A. Schreier and R.L. Baldwin, "Mechanism of Dissociation of S–peptide from Ribonuclease S."
Biochemistry 16, 4203–4209.
1978 T.Y. Tsong and R.L. Baldwin, "Effects of Solvent Viscosity and Different Guanidine Salts on the
Kinetics of Ribonuclease A Chain Folding." Biopolymers 17, 1669–1678.
1978 R.L. Baldwin, "The Pathway of Protein Folding." Trends Biochem. Sci. 3, 66–68.
1978 B.T. Nall, J.–R. Garel and R.L. Baldwin, "Test of the Extended Two–State Model for the Kinetic
Intermediates Observed in the Folding Transition of Ribonuclease A." J. Mol. Biol. 118, 317–
330.
1978 A.D. Blum, S.H. Smallcombe, and R.L. Baldwin, "Nuclear Magnetic Resonance Evidence for a
Structural Intermediate at an Early State in the Refolding of Ribonuclease A." J. Mol. Biol. 118,
305–316.
1978 F.X. Schmid and R.L. Baldwin, "Acid catalysis of the formation of the slow–folding species of
RNase A: Evidence that the reaction is proline isomerization." Proc. Natl. Acad. Sci. USA 75,
4764–4768.
1979 K.H. Cook, F.X. Schmid, and R.L. Baldwin, "Role of proline isomerization in folding of
ribonuclease A at low temperatures." Proc. Natl. Acad. Sci. USA 76, 6157–6161.
1979 F.X. Schmid and R.L. Baldwin, "The rate of interconversion between the two unfolded forms of
ribonuclease A does not depend on guanidinium chloride concentration." J. Mol. Biol. 133, 285–
287.
1979 F.X. Schmid and R.L. Baldwin, Nature of the slow–folding species of ribonuclease A. FEBS Fed.
Eur. Biochem. Soc. 12th Meeting, Dresden 1978, edited by E. Hofmann et al., Pergamon Press,
Oxford and New York, 1979.
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1979 P.J. Hagerman, F.X. Schmid and R.L. Baldwin. "Refolding Behavior of a Kinetic Intermediate
Observed in the Low pH Unfolding of Ribonuclease A." Biochemistry 18, 293–297.
1979 F.X. Schmid and R.L. Baldwin, "Detection of an Early Intermediate in the Folding of
Ribonuclease A by Protection of Amide Protons Against Exchange." J. Mol. Biol. 135, 199–215.
1979 A.M. Labhardt and R.L. Baldwin, "Recombination of S–Peptide with S–Protein During Folding
of Ribonuclease S. I. Folding Pathways of the Slow–Folding and Fast–Folding Classes of
Unfolded S–Protein." J. Mol. Biol. 135, 231–244.
1979 A.M. Labhardt and R.L. Baldwin, "Recombination of S–Peptide with S–Protein during Folding of
Ribonuclease S. II. Kinetic Characterization of a Stable Folding Intermediate Shown by S–Protein
at pH 1.7." J. Mol. Biol. 135, 245–254.
1979 R.L. Baldwin, "Discussions about Proteins." in Origins of Molecular Biology (recollections of
Jacques Monod) ed. by A. Lwoff and A. Ullmann, Academic Press, pp. 203-207.
1980 R.L. Baldwin and T.E. Creighton, "Recent Experimental work on the Pathway and Mechanism of
Protein Folding." In Protein Folding, R. Jaenicke, ed. Elsevier/North–Holland Biomedical Press,
pp. 217–260.
1980 R.L. Baldwin, "The Mechanism of Folding of Ribonucleases A and S." In Protein Folding,
R. Jaenicke, ed. Elsevier/North–Holland Biomedical Press, pp. 369–385.
1980 R.L. Baldwin, "Kinetic Intermediates and the Pathway of Folding of Ribonucleases A and S."
In Biomolecular Structure, Conformation, Function and Evolution, Vol. 2, Physico–Chemical and
Theoretical Studies, R. Srinivasan, ed. Pergamon Press Oxford and New York, pp. 87–96.
1980 J. Widom and R.L. Baldwin, "Cation–induced Toroidal Condensation of DNA. Studies with
Co3+(NH3)6." J. Mol. Biol. 144, 431–453.
1980 P.S. Kim and R.L. Baldwin, "Structural Intermediates Trapped during the Folding of
Ribonuclease A by Amide Proton Exchange." Biochemistry 19, 6124–6129.
1981 M. Jullien and R.L. Baldwin, "The Role of Proline Residues in the Folding Kinetics of the Bovine
Pancreatic Trypsin Inhibitor Derivative RCAM(14–38)." J. Mol. Biol. 145, 265–280.
1981 J.A. Ridge, R.L. Baldwin and A.M. Labhardt, "Nature of the Fast and Slow Refolding Reactions
of Iron(III) Cytochrome c." Biochemistry 20, 1622–1630.
1981 D. Shore, J. Langowski and R.L. Baldwin, "DNA flexibility studied by covalent closure of short
fragments into circles." Proc. Natl. Acad. Sci. USA 78, 4833–4837.
1982 P.S. Kim and R.L. Baldwin. "Influence of Charge on the Rate of Amide Proton Exchange".
Biochemistry 21, 1–5.
1982 P.S. Kim, A. Bierzynski and R.L. Baldwin. "A Competing Salt–Bridge Suppresses Helix
Formation by the Isolated C–peptide Carboxylate of Ribonuclease A". J. Mol. Biol. 162, 187–
199.
1982 P.S. Kim and R.L. Baldwin. "Specific intermediates in the folding reactions of small proteins and
the mechanism of protein folding". Ann. Rev. Biochem. 51, 459–489.
1982 A. Bierzynski, P.S. Kim and R.L. Baldwin. "A salt bridge stabilizes the helix formed by isolated
C–peptide of RNaseA". Proc. Natl. Acad. Sci. USA 79, 2470–2474.
1982 A. Bierzynski and R.L. Baldwin. "Local Secondary Structure in Ribonuclease A Denatured by
GuanidineHCl near 1oC". J. Mol. Biol. 162, 173–186.
1983 K. Kuwajima, P.S. Kim and R.L. Baldwin. "Strategy for Trapping Intermediates in the Folding of
Ribonuclease and for Using 1H–NMR to Determine Their Structures". Biopolymers 22, 59–67.
1983 J. Widom and R.L. Baldwin. "Monomolecular condensation of
Hexamine". Biopolymers 22, 1595–1620.
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1983 J. Widom and R.L. Baldwin. "Inhibition of Cation–Induced DNA Condensation by Intercalating
Dyes". Biopolymers 22, 1621–1632.
1983 A. Labhardt, J.A. Ridge, R.N. Lindquist and R.L. Baldwin. "Measurement of the Refolding
Combination Reaction between S–Peptide and S–Protein". Biochemistry 22, 321–327.
1983 K. Kuwajima and R.L. Baldwin. "Nature and Locations of the Most Slowly Exchanging Peptide
NH Protons in Residues 1 to 19 of Ribonuclease S". J. Mol. Biol. 169, 281–297.
1983 K. Kuwajima and R.L. Baldwin. "Exchange Behavior of the H–bonded Amide Protons in the 3 to
13 Helix of Ribonuclease S". J. Mol. Biol. 169, 299–323.
1983 D. Shore and R.L. Baldwin. "Energetics of DNA Twisting. I. Relation between Twist and
Cyclization Probability". J. Mol. Biol. 170, 957–981.
1983 D. Shore and R.L. Baldwin. "Energetics of DNA Twisting. II. Topoisomer Analysis". J. Mol.
Biol. 170, 983–1007.
1983 J. Widom and R.L. Baldwin. "Tests of Spool Models for DNA Packaging in Phage Lambda".
J. Mol. Biol. 171, 419–437.
1984 P.S. Kim and R.L. Baldwin. "A helix stop signal in the isolated S–peptide of ribonuclease A".
Nature 307, 329–334.
1984 F.X. Schmid, M.H. Buonocore and R.L. Baldwin. "Tests of the Simple Model of Lin and Brandts
for the Folding Kinetics of Ribonuclease A". Biochemistry 23, 3389–3394.
1984 D.N. Brems and R.L. Baldwin. "Amide Proton Exchange Used to Monitor the Formation of a
Stable –Helix by Residues 3 to 13 During Folding of Ribonuclease S". J. Mol. Biol. 180, 1141–
1156.
1985 K.R. Shoemaker, P.S. Kim, D.N. Brems, S. Marqusee, E.J. York, I.M. Chaiken, J.M. Stewart and
R.L. Baldwin. "Nature of the charged–group effect on the stability of the C–peptide helix". Proc.
Natl. Acad. Sci. USA 82, 2349–2353.
1985 D.N. Brems and R.L. Baldwin. "Protection of Amide Protons in Folding Intermediates of
Ribonuclease A Measured by pH–Pulse Exchange Curves". Biochemistry 24, 1689–1693.
1986 D. Loftus, G.O. Gbenle, P.S. Kim, R.L. Baldwin. "Effects of Denaturants on Amide Proton
Exchange Rates: A Test for Structure in Protein Fragments and Folding Intermediates".
Biochemistry 25, 1428–1436.
1986 C. Mitchinson and R.L. Baldwin. "The Design and Production of Semisynthetic Ribonucleases
With Increased Thermostability by Incorporation of S–Peptide Analogues With Enhanced Helical
Stability". Proteins: Structure, Function, and Genetics 1, 23–33.
1986 R.L. Baldwin. "Seeding Protein Folding". Trends in Biochem. Sci. 11, 6–9.
1986 R.L. Baldwin. "Protein Folding: Introductory Comments". In Methods in Enzymology, Vol. 131,
Academic Press, Inc., pp. 3–4.
1986 H. Utiyama and R.L. Baldwin. "Kinetic Mechanisms of Protein Folding. In Methods in
Enzymology, Vol. 131, Academic Press, Inc., pp. 51–70.
1986 R.L. Baldwin. "Workshop Report: Unfolding and Refolding Reactions of Proteins". Protein
Structure, Folding, and Design, pp. 247–248.
1986 R.L. Baldwin. "Temperature Dependence of the Hydrophobic Interaction in Protein Folding".
Proc. Natl. Acad. Sci., USA 83, 8069–8072.
1986 E.J. York, J.M. Stewart, R.L. Baldwin and K.R. Shoemaker, “Synthetic Helical Peptides.” In
Peptides, D. Theodoropoulos, ed., Walter de Gruyter & Co., Berlin, pp. 287-290.
1987 R.L. Baldwin. “Discussion of the Pathway of Protein Folding.” In Protein Structure, Folding,
and Design 2, Alan R. Liss, Inc., pp. 313–320.
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1987 K.R. Shoemaker, P.S. Kim, E.J. York, J.M. Stewart, R.L. Baldwin. "Tests of the helix dipole
model for stabilization of –Helices". Nature 326, 563–567.
1987 R.L. Baldwin and D. Eisenberg. "Protein Stability". In Protein Engineering. Alan R. Liss, Inc.,
pp. 127–148.
1987 K.R. Shoemaker, R. Fairman, P.S. Kim, E.J. York, J.M. Stewart and R.L. Baldwin. "The C–
peptide Helix from Ribonuclease A Considered as an Autonomous Folding Unit." Cold Spring
Harbor Symp. on Quantitative Biology, Vol. LII, pp. 391–398.
1987 S. Marqusee and R.L. Baldwin. "Helix stabilization by Glu–...Lys+ salt bridges in short peptides
of de novo design." Proc. Natl. Acad. Sci. USA 84, 8898–8902.
1988 K.R. Shoemaker, R. Fairman, E.J. York, J.M. Stewart and R.L. Baldwin. "Circular dichroism
measurement of peptide helix unfolding." Proc. Tenth American Peptide Symp., pp. 15–20.
1988 J.B. Udgaonkar and R.L. Baldwin. "NMR evidence of an early framework intermediate on the
folding pathway of ribonuclease A." Nature, 335, 694–699.
1988 R. Fairman, K.R. Shoemaker, E.J. York, J.M. Stewart and R.L. Baldwin. "Further Studies of the
Helix Dipole Model: Effects of a Free –NH3+ or –COO– Group on Helix Stability". Proteins
5, 1–7.
1989 F.M. Hughson and R.L. Baldwin. "Use of Site–Directed Mutagenesis To Destabilize Native
Apomyoglobin Relative to Folding Intermediates." Biochemistry 28, 4415–4422.
1989 K.G. Strehlow and R.L. Baldwin. "Effect of the Substitution Ala—> Gly at Each of Five Residue
Positions in the C–Peptide Helix." Biochemistry 28, 2130–2133.
1989 J.J. Osterhout, Jr., R.L. Baldwin, E.J. York, J.M. Stewart, H.J. Dyson and P.E. Wright. “1H NMR
Studies of the Solution Conformation of an Analogue of the C–peptide or Ribonuclease A”.
Biochemistry 28, 7059–7064.
1989 S. Marqusee, V.H. Robbins and R.L. Baldwin. "Unusually stable helix formation in short
alanine–based peptides". Proc. Natl. Acad. Sci. USA 86, 5286–5290.
1989 R.L. Baldwin. "How Does Protein Folding Get Started?" Trends Biochem. Sci. 14, 291–294.
1990 K.R. Shoemaker, R. Fairman, D.A. Schultz, A.D. Robertson, E.J. York. J.M. Stewart and R.L.
Baldwin. "Side–chain Interactions in the C–Peptide Helix: Phe 8...His 12+”. Biopolymers 29, 1–
11.
1990 S. Padmanabhan, S. Marqusee, T. Ridgeway, T.M. Laue and R.L. Baldwin. "Relative helix–
forming tendencies of nonpolar amino acids". Nature 344, 268–270.
1990 R. Fairman, K.R. Shoemaker, E.J. York, J.M. Stewart and R.L. Baldwin. "The Glu 2–...Arg 10+
side–chain interaction in the C–peptide helix of ribonuclease A". Biophys. Chem. 37, 107–119.
1990 P.S. Kim and R.L. Baldwin. "Intermediates in the Folding Reactions of Small Proteins". Ann.
Rev. Biochem. 59, 631–660.
1990 R.L. Baldwin. "Protein Folding and Stability", from Protein Design and the Development of New
Therapeutics and Vaccines (J.B. Hook and G. Poste, eds.). Plenum Publishing Corp., pp. 49-57.
1990 R.L. Baldwin. "Pieces of the folding puzzle". Nature 346, 409–410.
1990 J.B. Udgaonkar and R.L. Baldwin. "Early folding intermediate of ribonuclease A". Proc. Natl.
Acad. Sci. USA 87, 8197–8201.
1990 F.M. Hughson, P.E. Wright and R.L. Baldwin. "Structural Characterization of a Partly Folded
Apomyoglobin Intermediate". Science 249, 1544–1548.
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1990 S. Marqusee and Baldwin, R.L. "–Helix Formation by Short Peptides in Water" in "Protein
Folding: Deciphering the Second Half of the Genetic Code", L.M. Gierasch and J. King, eds.,
pp. 85–95. AAAS Press, Washington, D.C.
1991 R.L. Baldwin. "Experimental studies of pathways of protein folding". In Protein Conformation,
CIBA Foundation Symp. 161, D.J. Chadwick and K. Widdows, eds., Wiley and Sons, pp. 190–
205.
1991 J.M. Scholtz, S. Marqusee, R.L. Baldwin, E.J. York, J.M. Stewart, M. Santoro and D.W. Bolen.
"Calorimetric determination of the enthalpy change for the –helix to coil transition of an alanine
peptide in water." Proc. Natl. Acad. Sci. USA 88, 2854–2858.
1991 F.M. Hughson, D. Barrick and R.L. Baldwin. "Probing the Stability of a Partly Folded
Apomyoglobin Intermediate by Site–Directed Mutagenesis". Biochemistry 30, 4113–4118.
1991 S. Padmanabhan and R.L. Baldwin. "Straight–chain Non-polar Amino Acids are Good Helix–
formers in Water". J. Mol. Biol. 219, 135–137.
1991 K.G. Strehlow, A.D. Robertson and R.L. Baldwin. "Proline for Alanine Substitutions in the C–
Peptide Helix of Ribonuclease A". Biochemistry 30, 5810–5814.
1991 J.M. Scholtz, E.J. York, J.M. Stewart and R.L. Baldwin. "A Neutral, Water–Soluble, –Helical
Peptide: The Effect of Ionic Strength on the Helix–Coil Equilibrium". J. Amer. Chem. Soc., 113,
5102–5104.
1991 A. Chakrabartty, J.A. Schellman and R.L. Baldwin. "Large differences in the helix propensities of
alanine and glycine." Nature 351, 586–588.
1991 R. Fairman, K.M. Armstrong, K.R. Shoemaker, E.J. York, J.M. Stewart and R.L. Baldwin.
"Position Effect on Apparent Helical Propensities in the C–peptide Helix". J Mol. Biol. 221,
1395–1401.
1991 R.L. Baldwin and H. Roder. "Characterizing Protein Folding Intermediates." Current Biology 1,
218–220.
1991 A.D. Robertson and R.L. Baldwin. "Hydrogen Exchange in Thermally Denatured Ribonuclease
A." Biochemistry 30, 9907–9914.
1991 J.M. Scholtz, H. Qian, E.J. York, J.M. Stewart and R.L. Baldwin. "Parameters of Helix–Coil
Transition Theory for Alanine–Based Peptides of Varying Chain Lengths in Water." Biopolymers
31,1463–1470.
1991 R.L. Baldwin. "Molten Globules: Specific or Nonspecific Folding Intermediates?" Chemtracts
2, 379–389.
1992 C.A. Rohl, J.M. Scholtz, E.J. York, J.M. Stewart and R.L. Baldwin. "Kinetics of Amide Proton
Exchange in Helical Peptides of Varying Chain Lengths. Interpretation by the Lifson–Roig
Equation." Biochemistry 31, 1263–1269.
1992 J.M. Scholtz and R.L. Baldwin. "Mechanism of –Helix Formation by Peptides". Ann. Rev.
Biophys. Biomol. Struct. 21, 95–118.
1992 D.A. Schultz and R.L. Baldwin. "Cis proline mutants of ribonuclease A: I. Thermal stability."
Protein Science 1, 910–916.
1992 D.A. Schultz, F.X. Schmid and R.L. Baldwin. "Cis proline mutants of ribonuclease A:
II. Elimination of the slow–folding forms by mutation." Protein Science 1, 917–924.
1992 R.L. Baldwin and N. Muller. "Relation between the convergence temperatures T*h and T*s in
protein unfolding." Proc. Natl. Acad. Sci. USA 89, 7110–7113.
1993 K.M. Armstrong, R. Fairman and R.L. Baldwin. The (i, i+4) Phe–His Interaction Studied in an
Alanine–Based –Helix. J. Mol. Biol. 230, 284–291.
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1993 B.M.P. Huyghes–Despointes, J.M. Scholtz and R.L. Baldwin. Helical peptides with three pairs of
Asp–Arg and Glu–Arg residues in different orientations and spacings. Prot. Sci. 2, 80–85.
1993 A. Chakrabartty and R.L. Baldwin. Comparison of Amino Acid Helix Propensities (s–values) in
Different Experimental Systems. In Protein Folding: In Vivo and In Vitro, J.L. Cleland, ed.
Symposium of the American Chemical Society, pp. 166–177.
1993 D. Barrick and R.L. Baldwin. Three–State Analysis of Sperm Whale Apomyoglobin Folding.
Biochemistry 32, 3790–3796.
1993 R.L. Baldwin. Pulsed H/D–Exchange Studies of Folding Intermediates. Curr. Opin. Struc. Biol.
3, 84–91.
1993 J.M. Scholtz and R.L. Baldwin. Perchlorate–Induced Denaturation of Ribonuclease A:
Investigation of Possible Folding Intermediates. Biochemistry 32, 4604–4608.
1993 A. Chakrabartty, T. Kortemme, S. Padmanabhan and R.L. Baldwin. Aromatic Side–Chain
Contribution to Far–Ultraviolet Circular Dichroism of Helical Peptides and Its Effect on
Measurement of Helix Propensities. Biochemistry 32, 5560–5565.
1993 D. Barrick and R.L. Baldwin. The molten globule intermediate of apomyoglobin and the process
of protein folding. Protein Science 2, 869–876.
1993 J.M. Scholtz, H. Qian, V.H. Robbins and R.L. Baldwin. The Energetics of Ion–Pair and
Hydrogen–Bonding Interactions in a Helical Peptide. Biochemistry 32, 9668–9676.
1993 B.M.P. Huyghes–Despointes, J.M. Scholtz and R.L. Baldwin. Effect of a single aspartate on helix
stability at different positions in a neutral alanine–based peptide. Prot. Sci. 2, 1604–1611.
1993 S.L. Mayo and R.L. Baldwin. Guanidinium Chloride Induction of Partial Unfolding in Amide
Proton Exchange in RNase A. Science 262, 873–876.
1993 K.M. Armstrong and R.L. Baldwin. Charged histidine affects –helix stability at all positions in
the helix by interacting with the backbone charges. Proc. Natl. Acad. Sci. USA 90, 11337–11340.
1993 A. Chakrabartty, A.J. Doig and R.L. Baldwin. Helix capping propensities in peptides parallel
those in proteins. Proc. Natl. Acad. Sci. USA 90, 11332–11336.
1993 D.V. Laurents, A.J. Doig, D.A. Schultz and R.L. Baldwin. Characterization of a ribonuclease S
refolding intermediate. Phil. Trans. R. Soc. Lond. A. 345, 131–140.
1994 R.L. Baldwin, "Matching speed and stability." Nature 369, 183-184.
1994 A.J. Doig, A. Chakrabartty, T.M. Klingler and R.L. Baldwin. Determination of Free Energies of
N–Capping in –Helices by Modification of the Lifson–Roig Helix–Coil Theory To Include N–
and C–Capping. Biochemistry 33, 3396–3403.
1994 A. Chakrabartty, T. Kortemme and R.L. Baldwin. Helix propensities of the amino acids measured
in alanine–based peptides without helix–stabilizing side–chain interactions. Protein Science 3,
843–852.
1994 D. Barrick, F.M. Hughson and R.L. Baldwin. Molecular Mechanisms of Acid Denaturation.
J. Mol. Biol. 237, 588–601.
1994 S. Padmanabhan and R.L. Baldwin. Helix–stabilizing Interaction Between Tyrosine and Leucine
or Valine when the Spacing is i, i+4. J. Mol. Biol. 241, 706–713.
1994 S. Padmanabhan, E.J. York, L. Gera, J.M. Stewart and R.L. Baldwin. Helix–Forming Tendencies
of Amino Acids in Short (Hydroxybuytl)–L–glutamine Peptides: An Evaluation of the
Contradictory Results from Host–Guest Studies and Short Alanine–Based Peptides. Biochemistry
33, 8604–8609.
1994 S. Padmanabhan and R.L. Baldwin. Tests for helix-stabilizing interactions between various
nonpolar sidechains in alanine-based peptides. Protein Science 3, 1992-1997.
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1994 C.A. Rohl and R.L. Baldwin. Exchange Kinetics of Individual Amide Protons in 15N–Labeled
Helical Peptides Measured by Isotope–Edited NMR. Biochemistry 33, 7760–7767.
1994 R.L. Baldwin. Pathways and Mechanism of Protein Folding. In Statistical Mechanics, Protein
Structure, and Protein Substrate Interactions. S. Doniach, ed., Plenum Press, pp. 1–6.
1994 R.L. Baldwin, "Finding Intermediates in Protein Folding." BioEssays 16, 207-210.
1994 R.L. Baldwin and J.D. Ferry, "John Warren Williams 1898-1988." Biographical Memoirs 65,
374–389. National Academy Press.
1995 J.M. Scholtz, D. Barick, E.J. York, J.M. Stewart and R.L. Baldwin. Urea unfolding of peptide
helices as a model for interpreting protein unfolding. Proc. Natl. Acad. Sci. USA 92, 185–189.
1995 R.L. Baldwin. The nature of protein folding pathways: The classical versus the new view.
J. Biomolecular NMR 5, 103–109.
1995 J.B. Udgaonkar and R.L. Baldwin. Nature of the Early Folding Intermediate of Ribonuclease A.
Biochemistry 34, 4088–4096.
1995 T. Kiefhaber and R.L. Baldwin. Kinetics of hydrogen bond breakage in the process of unfolding
of ribonuclease A measured by pulsed hydrogen exchange. Proc. Natl. Acad. Sci. USA 92, 2657–
2661.
1995 A. Chakrabartty & R.L. Baldwin. Stability of –Helices. Adv. Protein Chem. 46, 141–176.
1995 T. Kiefhaber, A.M. Labhardt & R.L. Baldwin. Direct NMR Evidence for an Intermediate
Preceding the Rate–Limiting Step in the Unfolding of Ribonuclease A. Nature 375, 513–515.
1995 S.N. Loh, M.S. Kay and R.L. Baldwin. Structure and stability of a second molten globule
intermediate in the apomyoglobin folding pathway. Proc. Natl. Acad. Sci. USA 92, 5446–5450.
1995 R.L. Baldwin. –Helix formation by peptides of defined sequence. Biophys. Chem. 55, 127–135.
1995 T. Kiefhaber and R.L. Baldwin. Intrinsic Stability of Individual  Helices Modulates Structure
and Stability of the Apomyoglobin Molten Globule Form. J. Mol. Biol. 252, 122–132.
1995 B.M.P. Huyghues–Despointes, T.M. Klinger and R.L. Baldwin. Measuring the Strength of Side–
Chain Hydrogen Bonds in Peptide Helices: The Gln•Asp (i, i+4) Interaction. Biochemistry 34,
13267–13271.
1995 A.J. Doig and R.L. Baldwin. N– and C–capping preferences for all 20 amino acids in –helical
peptides. Prot. Sci. 4, 1325–1336.
1995 J.M. Scholtz and R.L. Baldwin, "-Helix Formation by Peptides in Water." In Peptides:
Synthesis, Structures and Applications. Academic Press, pp. 171-192.
1996 R.L. Baldwin. On–pathway versus off–pathway folding intermediates. Folding & Design 1, R1–
R8.
1996 S. Padmanabhan, E.J. York, J.M. Stewart and R.L. Baldwin. Helix Propensities of Basic Amino
Acids Increase with the Length of the Side–chain. J. Mol. Biol. 257, 726–734.
1996 S.N. Loh, C.A. Rohl, T. Kiefhaber and R.L. Baldwin. A general two–process model describes the
hydrogen exchange behavior of RNase A in unfolding conditions. Proc. Natl. Acad. Sci. USA 93,
1982–1987.
1996 R.L. Baldwin. Why is Protein Folding so Fast? Proc. Natl. Acad. Sci. USA 93, 2627–2628.
1996 Kay, M.S. and Baldwin, R.L. Packing interactions in the apomyoglobin folding intermediate.
Nature Struct. Biol. 3, 439–445.
1996 T. Kiefhaber and R.L. Baldwin. Hydrogen exchange and the unfolding pathway of ribonuclease
A. Biophys. Chem. 59, 351–356.
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1996 M. Jamin and R.L. Baldwin. Refolding and unfolding kinetics of the equilibrium folding
intermediate of apomyoglobin. Nature Struct. Biol. 3, 613–618.
1996 R.L. Baldwin. How Hofmeister Ion Interactions Affect Protein Stability. Biophys. J. 71, 2056–
2063.
1996 C.A. Rohl, A. Chakrabartty, R.L. Baldwin. Helix propagation and N-cap propensities of the
amino acids measured in alanine-based peptides in 40 volume percent trifluoroethanol. Protein
Sci. 5, 2623-2637.
1997 D. V. Laurents and R.L. Baldwin. Characterization of the Unfolding Pathway of Hen Egg White
Lysozyme. Biochemistry 36, 1496–1504.
1997 B.M.P. Huyghues–Despointes and R.L. Baldwin. Ion–Pair and Charged Hydrogen–Bond
Interactions between Histidine and Aspartate in a Peptide Helix. Biochemistry 36, 1965–1970.
1997 C.A. Rohl and R.L. Baldwin. Comparison of NH Exchange and Circular Dichroism as
Techniques for Measuring the Parameters of the Helix–Coil Transition in Peptides. Biochemistry
36, 8435–8442.
1997 R.L. Baldwin. The problem was to find the problem. Protein Science 6, 2031–2034.
1997 P. Luo and R.L. Baldwin. Mechanism of Helix Induction by Trifluoroethanol: A Framework for
Extrapolating the Helix–Forming Properties of Peptides from Trifluoroethanol/Water Mixtures
Back to Water. Biochemistry 36, 8413–8421.
1997 Y. Luo, M.S. Kay and R.L. Baldwin. Cooperativity of folding of the apomyoglobin pH 4
intermediate studied by glycine and proline mutations. Nature Struct. Biol. 4, 925–930.
1997 R.L. Baldwin. Competing unfolding pathways. Nature Struct. Biol. 4, 965–966.
1998 Y. Luo and R.L. Baldwin. Trifluoroethanol stabilizes the pH 4 folding intermediate of sperm
whale apomyoglobin. J. Mol. Biol. 279, 49–57.
1998 D.V. Laurents and R.L. Baldwin. Protein folding: matching theory and experiment. Biophys. J.
75, 428–434.
1998 M. Jamin and R.L. Baldwin. Two forms of the pH 4 folding intermediate of apomyoglobin.
J. Mol. Biol. 276, 491–504.
1998 J.M. Goldberg and R.L. Baldwin. Kinetic mechanism of a partial folding reaction. 1. Properties
of the reaction and effects of denaturants. Biochemistry 37, 2546–2555.
1998 J.M. Goldberg and R.L. Baldwin. Kinetic mechanism of a partial folding reaction. 2. Nature of
the transition state. Biochemistry 37, 2556–2563.
1998 B. Geierstanger, M. Jamin, B.F. Volkman, and R.L. Baldwin. Protonation behavior of histidine
24 and histidine 119 in forming the pH 4 folding intermediate of apomyoglobin. Biochemistry 37,
4254–4265.
1998 M.S. Kay and R.L. Baldwin. Alternative models for describing the acid unfolding of the
apomyoglobin folding intermediate. Biochemistry 37, 7859–7868.
1998 D.V. Laurents, M. Bruix, M. Jamin and R.L. Baldwin. A pulse–chase–competition experiment to
determine if a folding intermediate is on or off–pathway: application to ribonuclease A. J. Mol.
Biol. 283, 669–678.
1999 R.L. Baldwin and G.D. Rose. Is protein folding hierarchic? I. Local structure and peptide
folding. Trends Biochem. Sci. 24, 26–33.
1999 R.L. Baldwin and G.D. Rose. Is protein folding hierarchic? II. Folding intermediates and
transition states. Trends Biochem. Sci. 24, 77–83.
1999 M.S. Kay, C.H.I. Ramos, and R.L. Baldwin. Specificity of native–like interhelical hydrophobic
contacts in the apomyoglobin intermediate. Proc. Natl. Acad. Sci. USA 96, 2007–2012.
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1999 J.M. Goldberg and R.L. Baldwin. A specific transition state for S–peptide combining with folded
S–protein and then refolding. Proc. Natl. Acad. Sci. USA 96, 2019–2024.
1999 C.A. Rohl, W. Fiori, and R.L. Baldwin. Alanine is helix–stabilizing in both template–nucleated
and standard peptide helices. Proc. Natl. Acad. Sci. USA 96, 3682–3687.
1999 P. Luo and R.L. Baldwin. Interaction between water and polar groups of the helix backbone: An
important determinant of helix propensities. Proc. Natl. Acad. Sci. USA 96, 4930–4935.
1999 C.H.I. Ramos, M.S. Kay, and R.L. Baldwin. Putative Interhelix Ion Pairs Involved in the Stability
of Myoglobin. Biochemistry 38, 9783–9790.
1999 R.L. Baldwin . Oleg Ptitsyn 1929–1999. Protein Science 8, 1562–1563.
1999 Y. Luo and R.L. Baldwin. The 28–111 disulfide bond constrains the –lactalbumin molten
globule and weakens its cooperativity of folding. Proc. Natl. Acad. Sci. USA 96, 11283–11287.
1999 M. Jamin, S–R. Yeh, D.L. Rousseau and R.L. Baldwin. Submillisecond Unfolding Kinetics of
Apomyoglobin and its pH 4 Intermediate. J. Mol. Biol. 292, 731–740.
1999 R.L. Baldwin, "Protein Folding from 1961 to 1982." Nature Struct. Biol. 6, 814–817.
2000 F. Avbelj, P. Luo and R.L. Baldwin, "Energetics of the interaction between water and the helical
peptide group and its role in determining helix propensities." Proc. Natl. Acad. Sci. USA 97,
10786–10791.
2000 M. Jamin, M. Antalik, S.N. Loh, D.W. Bolen, and R.L. Baldwin. The unfolding enthalpy of the
pH 4 molten globule of apomyoglobin measured by isothermal titration calorimetry. Protein
Science 9, 1340–1346.
2000 R.L. Baldwin and B.H. Zimm. Are denatured proteins ever random coils? (Commentary). Proc.
Natl. Acad. Sci. USA 97, 12391–12392.
2001 R.L. Baldwin. Folding consensus? (News and Views) Nature Struct. Biol. 8, 92–93.
2001 Y. Luo and R.L. Baldwin, “How AlaGly Mutations in Different Helices Affect the Stability of
the Apomyoglobin Molten Globule.” Biochemistry 40, 5283–5289.
2001 M. Jamin, B. Geierstanger, and R.L. Baldwin, “The pKa of His–24 in the folding transition state
of apomyoglobin.” Proc. Natl. Acad. Sci. USA 98, 6127–6131.
2002 R.L. Baldwin, "Making a Network of Hydrophobic Clusters." Science 295, 1657–1658.
2002 M.M. Lopez, D.-H. Chin, R.L. Baldwin and G. Makhatadze, "The enthalpy of the alanine peptide
helix measured by isothermal titration calorimetry using metal binding to induce helix formation."
Proc. Natl. Acad. Sci. USA 99, 1298–1302.
2002 F. Avbelj an
propensities of the amino acids." Proc. Natl. Acad. Sci. USA 99, 1309–1313.
2002 Z. Shi, C.A. Olson, G.D. Rose, R.L. Baldwin and N.R. Kallenbach, "Polyproline II structure in a
sequence of seven alanine residues." Proc. Natl. Acad. Sci. USA 99, 9190–9195.
2002 C.H.I. Ramos and R.L. Baldwin, "Sulfate anion stabilization of native ribonuclease A both by
anion binding and by the Hofmeister effect." Protein Sci. 11, 1771–1778.
2002 P. Luo and R.L. Baldwin, "Origin of the different strengths of the (i,i+4) and (i,i+3) leucine pair
interactions in helices." Biophys. Chem. 96, 103–108.
2002 R.L. Baldwin, "A new perspective on unfolded proteins." Adv. Protein Chem. 62, 361–367.
2002 R.L. Baldwin, "John Schellman and his scientific work." Biophys. Chem. 101-102, 9–13.
2002 R.L. Baldwin, "Relation between peptide backbone solvation and the energetics of peptide
hydrogen bonds." Biophys. Chem. 101-102, 203–210.
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2002 D.-H. Chin, R.W. Woody, C.A. Rohl and R.L. Baldwin, "Circular dichroism spectra of short,
fixed–nucleus alanine helices." Proc. Natl. Acad. Sci. USA 99, 15416–15421.
2003 F. Avbelj and R.L. Baldwin, "Role of backbone solvation and electrostatics in generating
preferred peptide backbone conformations: distributions of phi." Proc. Natl. Acad. Sci. USA 100,
5742–5747.
2003 R.L. Baldwin, "In Search of the Energetic Role of Peptide Hydrogen Bonds." J. Biol. Chem. 278,
17581–17588.
2004 F. Avbelj and R.L. Baldwin, "Origin of the neighboring residue effect on peptide backbone
conformation." Proc. Natl. Acad. Sci. USA 101, 10967–10972.
2004 F. Avbelj, D. Kocjan, and R.L. Baldwin, "Protein chemical shifts arising from -helices and sheets depend on solvent exposure." Proc. Natl. Acad. Sci. USA 101, 17394–17397.
2005 R.L. Baldwin. “Early Days of Studying the Mechanism of Protein Folding.” In Protein Folding
Handbook. J. Buchner and T. Kiefhaber, eds., Wiley-VCH Verlag GmbH & Co. KgaA,
Weinheim, pp. 3–21.
2005 R.L. Baldwin. “Weak Interactions in Protein Folding: Hydrophobic Free Energy, van der Waals
Interactions, Peptide Hydrogen Bonds, and Peptide Solvation.” In Protein Folding Handbook.
J. Buchner and T. Kiefhaber, eds., Wiley-VCH Verlag GmbH & Co. KgaA, Weinheim, pp. 127–
162.
2006 F. Avbelj, S.G. Grdadolnik, J. Grdadolnik, and R.L. Baldwin, "Intrinsic backbone preferences are
fully present in blocked amino acids." Proc. Natl. Acad. Sci. USA 103, 1272–1277.
2006 R.L. Baldwin and D. Baker, eds. “Peptide Solvation and H-bonds”, Advances in Protein
Chemistry, Vol. 72, Academic Press (Elsevier), 312 pages.
2006 F. Avbelj and R.L. Baldwin. “Limited validity of group additivity for the folding energetics of the
peptide group.” Proteins 63, 283-289.
2007 R.L. Baldwin. “Energetics of Protein Folding.” J. Mol. Biol. 371, 283-301.
2008 R.L. Baldwin. “Recollections of Arthur Kornberg and the beginning of the Stanford Biochemistry
Department.” Protein Sci. 17, 385-388.
2008 R.L. Baldwin. “The search for folding intermediates and the mechanism of protein folding.”
Annu. Rev. Biophys. 37, 1-21.
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