Gas-liquid transfer data used to analyze hydrophobic hydration and
find the nature of the Kauzmann-Tanford hydrophobic factor.
Baldwin RL, Proc Natl Acad Sci U S A. 2012
Molten globules, entropy-driven conformational change and protein folding.
Baldwin RL, Rose GD. Curr Opin Struct Biol. 2012
Early days of protein hydrogen exchange: 1954-1972.
Baldwin RL, Proteins. 2011; 79 (7): 2021-6
Desolvation penalty for burying hydrogen-bonded peptide groups
in protein folding.
Baldwin RL, J Phys Chem B. 2010; 114 (49): 16223-7
Dry molten globule intermediates and the mechanism of protein unfolding.
Baldwin RL, Frieden C, Rose GD. Proteins. 2010; 78 (13): 2725-37
Helicity of short E-R/K peptides.
Sommese RF, Sivaramakrishnan S, Baldwin RL, Spudich JA. Protein Sci.
2010; 19 (10): 2001-5
In memoriam: Reflections on Fred Richards (1925-2009).
Baldwin RL, Protein Sci. 2009; 18 (4): 682-685
Recollections of Arthur Kornberg (1918-2007) and the beginning of the
Stanford Biochemistry Department.
Baldwin RL, Protein Sci. 2008; 17 (3): 385-8
The search for folding intermediates and the mechanism of protein folding.
Baldwin RL, Annu Rev Biophys. 2008: 37 1-21
Energetics of protein folding.
Baldwin RL, J Mol Biol. 2007; 371 (2): 283-301
Intrinsic backbone preferences are fully present in blocked amino acids.
Avbelj, F, Grdadolnik, SG, Grdadolnik, J, Baldwin, RL. Proc. Natl. Acad.
Sci. USA. 2006: 103 1272-1277
Peptide Solvation and H-bonds. Advances in Protein Chemistry, Vol. 72
Baldwin, RL, Baker, D, (eds.). Academic Press (Elsevier). 2006: 312 pages
Early Days of Studying the Mechanism of Protein Folding. In: Protein
Folding Handbook.
(J. Buchner and T. Kiefhaber, eds.)
Baldwin, RL, Wiley-VCH Verlag GmbH & Co. KgaA, Weinheim. 2005: pp. 3-21
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.). Baldwin. RL, Wiley-VCH Verlag GmbH & Co.
KgaA, Weinheim. 2005: 127-162
Origin of the neighboring residue effect on peptide backbone conformation.
Avbelj, F, Baldwin, RL. Proc Natl Acad Sci USA. 2004: 101 10967-10972
Protein chemical shifts arising from alpha-helices and beta-sheets depend
on solvent exposure.
Avbelj, F, Kocjan, D, Baldwin, RL. Proc. Natl. Acad. Sci. USA. 2004:
101 17394-17397
In search of the energetic role of peptide hydrogen bonds.
Baldwin RL, J Biol Chem. 2003; 278 (20): 17581-8
Role of backbone solvation and electrostatics in generating preferred
peptide backbone conformations: distributions of phi.
Avbelj, F, Baldwin, RL. Proc. Natl. Acad. Sci. USA. 2003: 100 5742-5747
A new perspective on unfolded proteins.
Baldwin RL, Adv Protein Chem. 2002: 62 361-7
Circular dichroism spectra of short, fixed-nucleus alanine helices.
Chin DH, Woody RW, Rohl CA, Baldwin RL. Proc Natl Acad Sci U S A.
2002; 99 (24): 15416-21
John Schellman and his scientific work.
Baldwin RL, Biophys Chem. 2002: 101-102 9-13
Limited validity of group additivity for the folding energetics of the peptide
group.
Avbelj, F, Baldwin, RL. Proteins. 2002: 99 9190-9195
Making a network of hydrophobic clusters.
Baldwin RL, Science. 2002; 295 (5560): 1657-8
Origin of the different strengths of the (i,i+4) and (i,i+3) leucine pair interactions
in helices.
Luo P, Baldwin RL. Biophys Chem. 2002; 96 (2-3): 103-8
Polyproline II structure in a sequence of seven alanine residues.
Shi, Z, Olson, CA, Rose, GD, Baldwin, RL, Kallenbach, NR. Proc Natl Acad Sci
USA. 2002: 99 9190-9195
Relation between peptide backbone solvation and the energetics of peptide
hydrogen bonds.
Baldwin RL, Biophys Chem. 2002: 101-102 203-10
Role of backbone solvation in determining thermodynamic propensities of the
amino acids.
Avbelj, F, Baldwin, RL. Proc. Natl. Acad. Sci. USA. 2002: 99 1309-1313
Sulfate anion stabilization of native ribonuclease A both by anion binding
and by the Hofmeister effect.
Ramos CH, Baldwin RL. Protein Sci. 2002; 11 (7): 1771-8
The enthalpy of the alanine peptide helix measured by isothermal titration
calorimetry using metal binding to induce helix formation.
Lopez, MM, Chin, D-H, Baldwin, RL, Makhatadze, G. Proc. Natl. Acad. Sci. USA.
2002: 99 1298-1302
Folding Consensus? (News and Views)
Baldwin, RL, Nat Struct Biol. 2001: 8 92-93
How Ala-->Gly mutations in different helices affect the stability of the
apomyoglobin molten globule.
Luo Y, Baldwin RL. Biochemistry. 2001; 40 (17): 5283-9
The pKa of His-24 in the folding transition state of apomyoglobin.
Jamin M, Geierstanger B, Baldwin RL. Proc Natl Acad Sci U S A. 2001;
98 (11): 6127-31
Are denatured proteins ever random coils?
Baldwin RL, Zimm BH. Proc Natl Acad Sci U S A. 2000; 97 (23): 12391-2
Energetics of the interaction between water and the helical peptide
group and its role in determining helix propensities.
Avbelj F, Luo P, Baldwin RL. Proc Natl Acad Sci U S A. 2000; 97 (20): 10786-91
The unfolding enthalpy of the pH 4 molten globule of apomyoglobin
measured by isothermal titration calorimetry.
Jamin M, Antalik M, Loh SN, Bolen DW, Baldwin RL. Protein Sci. 2000;
9 (7): 1340-6
A specific transition state for S-peptide combining with folded S-protein
and then refolding.
Goldberg JM, Baldwin RL. Proc Natl Acad Sci U S A. 1999; 96 (5): 2019-24
Interaction between water and polar groups of the helix backbone: an
important determinant of helix propensities.
Luo P, Baldwin RL. Proc Natl Acad Sci U S A. 1999; 96 (9): 4930-5
Is protein folding hierarchic? I. Local structure and peptide folding.
Baldwin RL, Rose GD. Trends Biochem Sci. 1999; 24 (1): 26-33
Is protein folding hierarchic? II. Folding intermediates and transition states.
Baldwin RL, Rose GD. Trends Biochem Sci. 1999; 24 (2): 77-83
Oleg Ptitsyn 1929-1999.
Baldwin RL, Protein Sci. 1999; 8 (7): 1562-3
Protein folding from 1961 to 1982.
Baldwin RL, Nat Struct Biol. 1999; 6 (9): 814-7
Putative interhelix ion pairs involved in the stability of myoglobin.
Ramos CH, Kay MS, Baldwin RL. Biochemistry. 1999; 38 (30): 9783-90
Specificity of native-like interhelical hydrophobic contacts in the apomyoglobin
intermediate.
Kay MS, Ramos CH, Baldwin RL. Proc Natl Acad Sci U S A. 1999; 96 (5): 2007-12
Submillisecond unfolding kinetics of apomyoglobin and its pH 4 intermediate.
Jamin M, Yeh SR, Rousseau DL, Baldwin RL. J Mol Biol. 1999; 292 (3): 731-40
The 28-111 disulfide bond constrains the alpha-lactalbumin molten globule
and weakens its cooperativity of folding.
Luo Y, Baldwin RL. Proc Natl Acad Sci U S A. 1999; 96 (20): 11283-7
A pulse-chase-competition experiment to determine if a folding intermediate
is on or off-pathway: application to ribonuclease A.
Laurents DV, Bruix M, Jamin M, Baldwin RL. J Mol Biol. 1998; 283 (3): 669-78
Alternative models for describing the acid unfolding of the apomyoglobin
folding intermediate.
Kay MS, Baldwin RL. Biochemistry. 1998; 37 (21): 7859-68
Kinetic mechanism of a partial folding reaction. 1. Properties Of the
reaction and effects of denaturants.
Goldberg JM, Baldwin RL. Biochemistry. 1998; 37 (8): 2546-55
Kinetic mechanism of a partial folding reaction. 2. Nature of the transition state.
Goldberg JM, Baldwin RL. Biochemistry. 1998; 37 (8): 2556-63
Protein folding: matching theory and experiment.
Laurents DV, Baldwin RL. Biophys J. 1998; 75 (1): 428-34
Protonation behavior of histidine 24 and histidine 119 in forming the pH 4
folding intermediate of apomyoglobin.
Geierstanger B, Jamin M, Volkman BF, Baldwin RL. Biochemistry. 1998;
37 (12): 4254-65
Trifluoroethanol stabilizes the pH 4 folding intermediate of sperm whale
apomyoglobin.
Luo Y, Baldwin RL. J Mol Biol. 1998; 279 (1): 49-57
Two forms of the pH 4 folding intermediate of apomyoglobin.
Jamin M, Baldwin RL. J Mol Biol. 1998; 276 (2): 491-504
Characterization of the unfolding pathway of hen egg white lysozyme.
Laurents DV, Baldwin RL. Biochemistry. 1997; 36 (6): 1496-504
Comparison of NH exchange and circular dichroism as techniques for
measuring the parameters of the helix-coil transition in peptides.
Rohl CA, Baldwin RL. Biochemistry. 1997; 36 (28): 8435-42
Cooperativity of folding of the apomyoglobin pH 4 intermediate studied by
glycine and proline mutations.
Luo Y, Kay MS, Baldwin RL. Nat Struct Biol. 1997; 4 (11): 925-30
Ion-pair and charged hydrogen-bond interactions between histidine and
aspartate in a peptide helix.
Huyghues-Despointes BM, Baldwin RL. Biochemistry. 1997; 36 (8): 1965-70
Mechanism of helix induction by trifluoroethanol: a framework for extrapolating
the helix-forming properties of peptides from trifluoroethanol/water mixtures
back to water.
Luo P, Baldwin RL. Biochemistry. 1997; 36 (27): 8413-21
The problem was to find the problem.
Baldwin RL, Protein Sci. 1997; 6 (9): 2031-4
A general two-process model describes the hydrogen exchange behavior of
RNase A in unfolding conditions.
Loh SN, Rohl CA, Kiefhaber T, Baldwin RL. Proc Natl Acad Sci U S A.
1996; 93 (5): 1982-7
Helix propagation and N-cap propensities of the amino acids measured in
alanine-based peptides in 40 volume percent trifluoroethanol.
Rohl CA, Chakrabartty A, Baldwin RL. Protein Sci. 1996; 5 (12): 2623-37
Helix propensities of basic amino acids increase with the length of the side-chain.
Padmanabhan S, York EJ, Stewart JM, Baldwin RL. J Mol Biol. 1996;
257 (3): 726-34
How Hofmeister ion interactions affect protein stability.
Baldwin RL, Biophys J. 1996; 71 (4): 2056-63
On-pathway versus off-pathway folding intermediates.
Baldwin RL, Fold Des. 1996; 1 (1): R1-8
Packing interactions in the apomyglobin folding intermediate.
Kay MS, Baldwin RL. Nat Struct Biol. 1996; 3 (5): 439-45
Refolding and unfolding kinetics of the equilibrium folding intermediate of
apomyoglobin.
Jamin M, Baldwin RL. Nat Struct Biol. 1996; 3 (7): 613-8
Alpha-helix formation by peptides of defined sequence.
Baldwin RL, Biophys Chem. 1995 Jun-Jul; 55 (1-2): 127-35
Intrinsic stability of individual alpha helices modulates structure and stability
of the apomyoglobin molten globule form.
Kiefhaber T, Baldwin RL. J Mol Biol. 1995; 252 (1): 122-32
Kinetics of hydrogen bond breakage in the process of unfolding of ribonuclease
A measured by pulsed hydrogen exchange.
Kiefhaber T, Baldwin RL. Proc Natl Acad Sci U S A. 1995; 92 (7): 2657-61
Measuring the strength of side-chain hydrogen bonds in peptide helices: the
Gln.Asp (i, i + 4) interaction.
Huyghues-Despointes BM, Klingler TM, Baldwin RL. Biochemistry. 1995;
34 (41): 13267-71
Nature of the early folding intermediate of ribonuclease A.
Udgaonkar JB, Baldwin RL. Biochemistry. 1995; 34 (12): 4088-96
Stability of alpha-helices.
Chakrabartty A, Baldwin RL. Adv Protein Chem. 1995: 46 141-76
Structure and stability of a second molten globule intermediate in the apomyoglobin
folding pathway.
Loh SN, Kay MS, Baldwin RL. Proc Natl Acad Sci U S A. 1995; 92 (12): 5446-50
The nature of protein folding pathways: the classical versus the new view.
Baldwin RL, J Biomol NMR. 1995; 5 (2): 103-9
Urea unfolding of peptide helices as a model for interpreting protein unfolding.
Scholtz JM, Barrick D, York EJ, Stewart JM, Baldwin RL. Proc Natl Acad Sci U S A.
1995; 92 (1): 185-9
Determination of free energies of N-capping in alpha-helices by modification
of the Lifson-Roig helix-coil therapy to include N- and C-capping.
Doig AJ, Chakrabartty A, Klingler TM, Baldwin RL. Biochemistry. 1994;
33 (11): 3396-403
Exchange kinetics of individual amide protons in 15N-labeled helical peptides
measured by isotope-edited NMR.
Rohl CA, Baldwin RL. Biochemistry. 1994; 33 (25): 7760-7
Finding intermediates in protein folding.
Baldwin RL, Bioessays. 1994; 16 (3): 207-10
Helix propensities of the amino acids measured in alanine-based peptides
without helix-stabilizing side-chain interactions.
Chakrabartty A, Kortemme T, Baldwin RL. Protein Sci. 1994; 3 (5): 843-52
Helix-forming tendencies of amino acids in short (hydroxybutyl)-L-glutamine
peptides: an evaluation of the contradictory results from host-guest studies
and short alanine-based peptides.
Padmanabhan S, York EJ, Gera L, Stewart JM, Baldwin RL. Biochemistry.
1994; 33 (28): 8604-9
Helix-stabilizing interaction between tyrosine and leucine or valine when the
spacing is i, i + 4.
Padmanabhan S, Baldwin RL. J Mol Biol. 1994; 241 (5): 706-13
Molecular mechanisms of acid denaturation. The role of histidine residues in
the partial unfolding of apomyoglobin.
Barrick D, Hughson FM, Baldwin RL. J Mol Biol. 1994; 237 (5): 588-601
Tests for helix-stabilizing interactions between various nonpolar side chains in
alanine-based peptides.
Padmanabhan S, Baldwin RL. Protein Sci. 1994; 3 (11): 1992-7
Aromatic side-chain contribution to far-ultraviolet circular dichroism of helical
peptides and its effect on measurement of helix propensities.
Chakrabartty A, Kortemme T, Padmanabhan S, Baldwin RL. Biochemistry.
1993; 32 (21): 5560-5
Charged histidine affects alpha-helix stability at all positions in the helix by
interacting with the backbone charges.
Armstrong KM, Baldwin RL. Proc Natl Acad Sci U S A. 1993; 90 (23): 11337-40
Effect of a single aspartate on helix stability at different positions in a neutral
alanine-based peptide.
Huyghues-Despointes BM, Scholtz JM, Baldwin RL. Protein Sci. 1993;
2 (10): 1604-11
Guanidinium chloride induction of partial unfolding in amide proton exchange
in RNase A.
Mayo SL, Baldwin RL. Science. 1993; 262 (5135): 873-6
Helical peptides with three pairs of Asp-Arg and Glu-Arg residues in different
orientations and spacings.
Huyghues-Despointes BM, Scholtz JM, Baldwin RL. Protein Sci. 1993; 2 (1): 80-5
Helix capping propensities in peptides parallel those in proteins.
Chakrabartty A, Doig AJ, Baldwin RL. Proc Natl Acad Sci U S A. 1993;
90 (23): 11332-6
Perchlorate-induced denaturation of ribonuclease A: investigation of possible
folding intermediates.
Scholtz JM, Baldwin RL. Biochemistry. 1993; 32 (17): 4604-8
Stein and Moore Award address. The molten globule intermediate of apomyoglobin
and the process of protein folding.
Barrick D, Baldwin RL. Protein Sci. 1993; 2 (6): 869-76
The (i, i + 4) Phe-His interaction studied in an alanine-based alpha-helix.
Armstrong KM, Fairman R, Baldwin RL. J Mol Biol. 1993; 230 (1): 284-91
The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide.
Scholtz JM, Qian H, Robbins VH, Baldwin RL. Biochemistry. 1993; 32 (37): 9668-76
Three-state analysis of sperm whale apomyoglobin folding.
Barrick D, Baldwin RL. Biochemistry. 1993; 32 (14): 3790-6
Cis proline mutants of ribonuclease A. I. Thermal stability.
Schultz DA, Baldwin RL. Protein Sci. 1992; 1 (7): 910-6
Cis proline mutants of ribonuclease A. II. Elimination of the slow-folding forms
by mutation.
Schultz DA, Schmid FX, Baldwin RL. Protein Sci. 1992; 1 (7): 917-24
Kinetics of amide proton exchange in helical peptides of varying chain lengths.
Interpretation by the Lifson-Roig equation.
Rohl CA, Scholtz JM, York EJ, Stewart JM, Baldwin RL. Biochemistry.
1992; 31 (5): 1263-9
Relation between the convergence temperatures Th* and Ts* in protein unfolding.
Baldwin RL, Muller N. Proc Natl Acad Sci U S A. 1992; 89 (15): 7110-3
The mechanism of alpha-helix formation by peptides.
Scholtz JM, Baldwin RL. Annu Rev Biophys Biomol Struct. 1992: 21 95-118
Calorimetric determination of the enthalpy change for the alpha-helix to coil
transition of an alanine peptide in water.
Scholtz JM, Marqusee S, Baldwin RL, York EJ, Stewart JM, Santoro M,
Bolen DW. Proc Natl Acad Sci U S A. 1991; 88 (7): 2854-8
Characterizing protein folding intermediates.
Baldwin RL, Roder H. Curr Biol. 1991; 1 (4): 218-20
Experimental studies of pathways of protein folding.
Baldwin RL, Ciba Found Symp. 1991: 161 190-201; discussion 201-5
Hydrogen exchange in thermally denatured ribonuclease A.
Robertson AD, Baldwin RL. Biochemistry. 1991; 30 (41): 9907-14
Large differences in the helix propensities of alanine and glycine.
Chakrabartty A, Schellman JA, Baldwin RL. Nature. 1991; 351 (6327): 586-8
Parameters of helix-coil transition theory for alanine-based peptides of varying
chain lengths in water.
Scholtz JM, Qian H, York EJ, Stewart JM, Baldwin RL. Biopolymers.
1991; 31 (13): 1463-70
Position effect on apparent helical propensities in the C-peptide helix.
Fairman R, Armstrong KM, Shoemaker KR, York EJ, Stewart JM, Baldwin RL.
J Mol Biol. 1991; 221 (4): 1395-401
Probing the stability of a partly folded apomyoglobin intermediate by site-directed
mutagenesis.
Hughson FM, Barrick D, Baldwin RL. Biochemistry. 1991; 30 (17): 4113-8
Proline for alanine substitutions in the C-peptide helix of ribonuclease A.
Strehlow KG, Robertson AD, Baldwin RL. Biochemistry. 1991; 30 (23): 5810-4
Straight-chain non-polar amino acids are good helix-formers in water.
Padmanabhan S, Baldwin RL. J Mol Biol. 1991; 219 (2): 135-7
Early folding intermediate of ribonuclease A.
Udgaonkar JB, Baldwin RL. Proc Natl Acad Sci U S A. 1990; 87 (21): 8197-201
Relative helix-forming tendencies of nonpolar amino acids.
Padmanabhan S, Marqusee S, Ridgeway T, Laue TM, Baldwin RL. Nature. 1990;
344 (6263): 268-70
Side-chain interactions in the C-peptide helix: Phe 8 ... His 12+.
Shoemaker KR, Fairman R, Schultz DA, Robertson AD, York EJ, Stewart JM,
Baldwin RL. Biopolymers. 1990; 29 (1): 1-11
Structural characterization of a partly folded apomyoglobin intermediate.
Hughson FM, Wright PE, Baldwin RL. Science. 1990; 249 (4976): 1544-8
The Glu 2- ... Arg 10+ side-chain interaction in the C-peptide helix of ribonuclease A.
Fairman R, Shoemaker KR, York EJ, Stewart JM, Baldwin RL. Biophys Chem.
1990; 37 (1-3): 107-19
1H NMR studies of the solution conformations of an analogue of the C-peptide
of ribonuclease A.
Osterhout JJ, Baldwin RL, York EJ, Stewart JM, Dyson HJ, Wright PE.
Biochemistry. 1989; 28 (17): 7059-64
Effect of the substitution Ala-Gly at each of five residue positions in the
C-peptide helix.
Strehlow KG, Baldwin RL. Biochemistry. 1989; 28 (5): 2130-3
Further studies of the helix dipole model: effects of a free alpha-NH3+ or
alpha-COO- group on helix stability.
Fairman R, Shoemaker KR, York EJ, Stewart JM, Baldwin RL. Proteins.
1989; 5 (1): 1-7
Unusually stable helix formation in short alanine-based peptides.
Marqusee S, Robbins VH, Baldwin RL. Proc Natl Acad Sci U S A. 1989; 86
(14): 5286-90
Use of site-directed mutagenesis to destabilize native apomyoglobin relative to
folding intermediates.
Hughson FM, Baldwin RL. Biochemistry. 1989; 28 (10): 4415-22
NMR evidence for an early framework intermediate on the folding pathway of
ribonuclease A.
Udgaonkar JB, Baldwin RL. Nature. 1988; 335 (6192): 694-9
Helix stabilization by Glu-...Lys+ salt bridges in short peptides of de novo design.
Marqusee S, Baldwin RL. Proc Natl Acad Sci U S A. 1987; 84 (24): 8898-902
The C-peptide helix from ribonuclease A considered as an autonomous folding unit.
Shoemaker KR, Fairman R, Kim PS, York EJ, Stewart JM, Baldwin RL. Cold Spring
Harb Symp Quant Biol. 1987: 52 391-8
The design and production of semisynthetic ribonucleases with increased
thermostability by incorporation of S-peptide analogues with enhanced helical
stability.
Mitchinson C, Baldwin RL. Proteins. 1986; 1 (1): 23-33