Publications
-
Molten globules, entropy-driven conformational change and protein folding.
Baldwin RL,
Rose GD.
Curr Opin Struct Biol.
2013;
23
(1):
4-10
-
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;
109
(19):
7310-3
-
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
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