Robert Lesh Baldwin - Publications

Affiliations: 
Biochemistry Stanford University, Palo Alto, CA 
Area:
Energetics of protein folding
Website:
http://rbaldwin.stanford.edu/BaldwinBio.html

133 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2016 Baldwin RL, Rose GD. How the hydrophobic factor drives protein folding. Proceedings of the National Academy of Sciences of the United States of America. PMID 27791131 DOI: 10.1073/pnas.1610541113  0.52
2014 Baldwin RL. Dynamic hydration shell restores Kauzmann's 1959 explanation of how the hydrophobic factor drives protein folding. Proceedings of the National Academy of Sciences of the United States of America. 111: 13052-6. PMID 25157156 DOI: 10.1073/pnas.1414556111  1
2013 Baldwin RL. The new view of hydrophobic free energy. Febs Letters. 587: 1062-6. PMID 23337880 DOI: 10.1016/j.febslet.2013.01.006  1
2013 Baldwin RL. Properties of hydrophobic free energy found by gas-liquid transfer. Proceedings of the National Academy of Sciences of the United States of America. 110: 1670-3. PMID 23319615 DOI: 10.1073/pnas.1220825110  1
2013 Baldwin RL, Rose GD. Molten globules, entropy-driven conformational change and protein folding. Current Opinion in Structural Biology. 23: 4-10. PMID 23237704 DOI: 10.1016/j.sbi.2012.11.004  1
2012 Baldwin RL. Gas-liquid transfer data used to analyze hydrophobic hydration and find the nature of the Kauzmann-Tanford hydrophobic factor. Proceedings of the National Academy of Sciences of the United States of America. 109: 7310-3. PMID 22529345 DOI: 10.1073/pnas.1203720109  1
2011 Baldwin RL. Early days of protein hydrogen exchange: 1954-1972. Proteins. 79: 2021-6. PMID 21557321 DOI: 10.1002/prot.23039  1
2011 Grdadolnik J, Mohacek-Grosev V, Baldwin RL, Avbelj F. Populations of the three major backbone conformations in 19 amino acid dipeptides. Proceedings of the National Academy of Sciences of the United States of America. 108: 1794-8. PMID 21205907 DOI: 10.1073/pnas.1017317108  1
2010 Baldwin RL. Desolvation penalty for burying hydrogen-bonded peptide groups in protein folding. The Journal of Physical Chemistry. B. 114: 16223-7. PMID 20961078 DOI: 10.1021/jp107111f  1
2010 Sommese RF, Sivaramakrishnan S, Baldwin RL, Spudich JA. Helicity of short E-R/K peptides. Protein Science : a Publication of the Protein Society. 19: 2001-5. PMID 20669185 DOI: 10.1002/pro.469  1
2010 Baldwin RL, Frieden C, Rose GD. Dry molten globule intermediates and the mechanism of protein unfolding. Proteins. 78: 2725-37. PMID 20635344 DOI: 10.1002/prot.22803  1
2009 Avbelj F, Baldwin RL. Origin of the change in solvation enthalpy of the peptide group when neighboring peptide groups are added. Proceedings of the National Academy of Sciences of the United States of America. 106: 3137-41. PMID 19202077 DOI: 10.1073/pnas.0813018106  1
2008 Baldwin RL. The search for folding intermediates and the mechanism of protein folding. Annual Review of Biophysics. 37: 1-21. PMID 18573070 DOI: 10.1146/annurev.biophys.37.032807.125948  1
2008 Baldwin RL. Recollections of Arthur Kornberg (1918-2007) and the beginning of the Stanford Biochemistry Department. Protein Science : a Publication of the Protein Society. 17: 385-8. PMID 18350670 DOI: 10.1002/pro.170385  1
2008 Baldwin RL. Weak Interactions in Protein Folding: Hydrophobic Free Energy, van der Waals Interactions, Peptide Hydrogen Bonds, and Peptide Solvation Protein Folding Handbook. 1: 127-162. DOI: 10.1002/9783527619498.ch6  1
2008 Baldwin RL. Early Days of Studying the Mechanism of Protein Folding Protein Folding Handbook. 1: 1-21. DOI: 10.1002/9783527619498.ch1  1
2007 Baldwin RL. Energetics of protein folding. Journal of Molecular Biology. 371: 283-301. PMID 17582437 DOI: 10.1016/j.jmb.2007.05.078  1
2006 Avbelj F, Grdadolnik SG, Grdadolnik J, Baldwin RL. Intrinsic backbone preferences are fully present in blocked amino acids. Proceedings of the National Academy of Sciences of the United States of America. 103: 1272-7. PMID 16423894 DOI: 10.1073/pnas.0510420103  1
2006 Avbelj F, Baldwin RL. Limited validity of group additivity for the folding energetics of the peptide group. Proteins. 63: 283-9. PMID 16288449 DOI: 10.1002/prot.20756  1
2004 Avbelj F, Kocjan D, Baldwin RL. Protein chemical shifts arising from alpha-helices and beta-sheets depend on solvent exposure. Proceedings of the National Academy of Sciences of the United States of America. 101: 17394-7. PMID 15574491 DOI: 10.1073/pnas.0407969101  1
2004 Avbelj F, Baldwin RL. Origin of the neighboring residue effect on peptide backbone conformation. Proceedings of the National Academy of Sciences of the United States of America. 101: 10967-72. PMID 15254296 DOI: 10.1073/pnas.0404050101  1
2003 Avbelj F, Baldwin RL. Role of backbone solvation and electrostatics in generating preferred peptide backbone conformations: distributions of phi. Proceedings of the National Academy of Sciences of the United States of America. 100: 5742-7. PMID 12709596 DOI: 10.1073/pnas.1031522100  1
2003 Baldwin RL. In search of the energetic role of peptide hydrogen bonds. The Journal of Biological Chemistry. 278: 17581-8. PMID 12582164 DOI: 10.1074/jbc.X200009200  1
2002 Baldwin RL. Relation between peptide backbone solvation and the energetics of peptide hydrogen bonds. Biophysical Chemistry. 101: 203-10. PMID 12488001 DOI: 10.1016/S0301-4622(02)00195-3  1
2002 Baldwin RL. John Schellman and his scientific work. Biophysical Chemistry. 101: 9-13. PMID 12487983  1
2002 Chin DH, Woody RW, Rohl CA, Baldwin RL. Circular dichroism spectra of short, fixed-nucleus alanine helices. Proceedings of the National Academy of Sciences of the United States of America. 99: 15416-21. PMID 12427967 DOI: 10.1073/pnas.232591399  1
2002 Baldwin RL. A new perspective on unfolded proteins. Advances in Protein Chemistry. 62: 361-7. PMID 12418110 DOI: 10.1016/S0065-3233(02)62014-5  1
2002 Shi Z, Olson CA, Rose GD, Baldwin RL, Kallenbach NR. Polyproline II structure in a sequence of seven alanine residues. Proceedings of the National Academy of Sciences of the United States of America. 99: 9190-5. PMID 12091708 DOI: 10.1073/pnas.112193999  1
2002 Ramos CH, Baldwin RL. Sulfate anion stabilization of native ribonuclease A both by anion binding and by the Hofmeister effect. Protein Science : a Publication of the Protein Society. 11: 1771-8. PMID 12070329 DOI: 10.1110/ps.0205902  1
2002 Luo P, Baldwin RL. Origin of the different strengths of the (i,i+4) and (i,i+3) leucine pair interactions in helices. Biophysical Chemistry. 96: 103-8. PMID 12034432 DOI: 10.1016/S0301-4622(02)00010-8  1
2002 Baldwin RL. Making a network of hydrophobic clusters. Science (New York, N.Y.). 295: 1657-8. PMID 11872825 DOI: 10.1126/science.1069893  1
2002 Lopez MM, Chin DH, Baldwin RL, Makhatadze GI. The enthalpy of the alanine peptide helix measured by isothermal titration calorimetry using metal-binding to induce helix formation. Proceedings of the National Academy of Sciences of the United States of America. 99: 1298-302. PMID 11818561 DOI: 10.1073/pnas.032665199  1
2002 Avbelj F, Baldwin RL. Role of backbone solvation in determining thermodynamic beta propensities of the amino acids. Proceedings of the National Academy of Sciences of the United States of America. 99: 1309-13. PMID 11805303 DOI: 10.1073/pnas.032665499  1
2002 Qian H, Hofrichter J, Baldwin RL. Biophysical chemistry of proteins and nucleic acids: A festschrift for John A. Schellman Biophysical Chemistry. 101: 7-8. DOI: 10.1016/S0301-4622(02)00185-0  1
2001 Jamin M, Geierstanger B, Baldwin RL. The pKa of His-24 in the folding transition state of apomyoglobin. Proceedings of the National Academy of Sciences of the United States of America. 98: 6127-31. PMID 11353859 DOI: 10.1073/pnas.111157998  1
2001 Baldwin RL. Folding consensus? Nature Structural Biology. 8: 92-4. PMID 11175886 DOI: 10.1038/84189  1
2001 Luo Y, Baldwin RL. How Ala→Gly mutations in different helices affect the stability of the apomyoglobin molten globule Biochemistry. 40: 5283-5289.  1
2000 Baldwin RL, Zimm BH. Are denatured proteins ever random coils? Proceedings of the National Academy of Sciences of the United States of America. 97: 12391-2. PMID 11070072 DOI: 10.1073/pnas.97.23.12391  1
2000 Avbelj F, Luo P, Baldwin RL. Energetics of the interaction between water and the helical peptide group and its role in determining helix propensities Proceedings of the National Academy of Sciences of the United States of America. 97: 10786-10791. PMID 10984522  1
2000 Jamin M, Antalik M, Loh SN, Bolen DW, Baldwin RL. The unfolding enthalpy of the pH 4 molten globule of apomyoglobin measured by isothermal titration calorimetry Protein Science. 9: 1340-1346. PMID 10933499  1
1999 Luo Y, Baldwin RL. The 28-111 disulfide bond constrains the α-lactalbumin molten globule and weakens its cooperativity of folding Proceedings of the National Academy of Sciences of the United States of America. 96: 11283-11287. PMID 10500168 DOI: 10.1073/pnas.96.20.11283  1
1999 Jamin M, Yeh SR, Rousseau DL, Baldwin RL. Submillisecond unfolding kinetics of apomyoglobin and its pH 4 intermediate. Journal of Molecular Biology. 292: 731-40. PMID 10497035 DOI: 10.1006/jmbi.1999.3074  1
1999 Baldwin RL. Protein folding from 1961 to 1982 Nature Structural Biology. 6: 814-817. PMID 10467090  1
1999 Ramos CHI, Kay MS, Baldwin RL. Putative interhelix ion Pairs involved in the stability of myoglobin Biochemistry. 38: 9783-9790. PMID 10423259 DOI: 10.1021/bi9828627  1
1999 Baldwin RL. Oleg Ptitsyn 1929-1999 Protein Science : a Publication of the Protein Society. 8: 1562-1563. PMID 10422848  1
1999 Luo P, Baldwin RL. Interaction between water and polar groups of the helix backbone: An important determinant of helix propensities Proceedings of the National Academy of Sciences of the United States of America. 96: 4930-4935. PMID 10220396 DOI: 10.1073/pnas.96.9.4930  1
1999 Baldwin RL, Rose GD. Is protein folding hierarchic? II. Folding intermediates and transition states Trends in Biochemical Sciences. 24: 77-83. PMID 10098403 DOI: 10.1016/S0968-0004(98)01345-0  1
1999 Rohl CA, Fiori W, Baldwin RL. Alanine is helix-stabilizing in both template-nucleated and standard peptide helices. Proceedings of the National Academy of Sciences of the United States of America. 96: 3682-7. PMID 10097097 DOI: 10.1073/pnas.96.7.3682  1
1999 Baldwin RL, Rose GD. Is protein folding hierarchic? I. Local structure and peptide folding Trends in Biochemical Sciences. 24: 26-33. PMID 10087919 DOI: 10.1016/S0968-0004(98)01346-2  1
1999 Goldberg JM, Baldwin RL. A specific transition state for S-peptide combining with folded S-protein and then refolding. Proceedings of the National Academy of Sciences of the United States of America. 96: 2019-24. PMID 10051587 DOI: 10.1073/pnas.96.5.2019  1
1999 Kay MS, Ramos CHI, Baldwin RL. Specificity of native-like interhelical hydrophobic contacts in the apomyoglobin intermediate Proceedings of the National Academy of Sciences of the United States of America. 96: 2007-2012. PMID 10051585 DOI: 10.1073/pnas.96.5.2007  1
1998 Laurents DV, Bruix M, Jamin M, Baldwin RL. A pulse-chase-competition experiment to determine if a folding intermediate is on or off-pathway: Application to ribonuclease A Journal of Molecular Biology. 283: 669-678. PMID 9784375 DOI: 10.1006/jmbi.1998.2118  1
1998 Rohl CA, Baldwin RL. Deciphering rules of helix stability in peptides. Methods in Enzymology. 295: 1-26. PMID 9750211 DOI: 10.1016/S0076-6879(98)95032-7  1
1998 Laurents DV, Baldwin RL. Protein folding: Matching theory and experiment Biophysical Journal. 75: 428-434. PMID 9649403  1
1998 Luo Y, Baldwin RL. Trifluoroethanol stabilizes the pH 4 folding intermediate of sperm whale apomyoglobin Journal of Molecular Biology. 279: 49-57. PMID 9636699 DOI: 10.1006/jmbi.1998.1774  1
1998 Kay MS, Baldwin RL. Alternative models for describing the acid unfolding of the apomyoglobin folding intermediate Biochemistry. 37: 7859-7868. PMID 9601047 DOI: 10.1021/bi9802061  1
1998 Jamin M, Baldwin RL. Two forms of the pH 4 folding intermediate of apomyoglobin Journal of Molecular Biology. 276: 491-504. PMID 9512718 DOI: 10.1006/jmbi.1997.1543  1
1998 Goldberg JM, Baldwin RL. Kinetic mechanism of a partial folding reaction. 2. Nature of the transition state. Biochemistry. 37: 2556-63. PMID 9485405 DOI: 10.1021/bi972403q  1
1998 Goldberg JM, Baldwin RL. Kinetic mechanism of a partial folding reaction. 1. Properties Of the reaction and effects of denaturants. Biochemistry. 37: 2546-55. PMID 9485404 DOI: 10.1021/bi972402y  1
1997 Baldwin RL. Competing unfolding pathways Nature Structural Biology. 4: 965-966. PMID 9406539  1
1997 Luo Y, Kay MS, Baldwin RL. Cooperativity of folding of the apomyoglobin pH 4 intermediate studied by glycine and proline mutations Nature Structural Biology. 4: 925-930. PMID 9360609 DOI: 10.1038/nsb1197-925  1
1997 Baldwin RL. The problem was to find the problem Protein Science : a Publication of the Protein Society. 6: 2031-2034. PMID 9300503  1
1997 Rohl CA, Baldwin RL. Comparison of NH exchange and circular dichroism as techniques for measuring the parameters of the helix-coil transition in peptides. Biochemistry. 36: 8435-42. PMID 9214287 DOI: 10.1021/bi9706677  1
1997 Luo P, Baldwin RL. 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. PMID 9204889 DOI: 10.1021/bi9707133  1
1997 Laurents DV, Baldwin RL. Characterization of the unfolding pathway of hen egg white lysozyme Biochemistry. 36: 1496-1504. PMID 9063898 DOI: 10.1021/bi962198z  1
1997 Huyghues-Despointes BMP, Baldwin RL. Ion-pair and charged hydrogen-bond interactions between histidine and aspartate in a peptide helix Biochemistry. 36: 1965-1970. PMID 9047293 DOI: 10.1021/bi962546x  1
1997 Baldwin RL. Intermediates on the folding pathway of apomyoglobin Faseb Journal. 11: A1006.  1
1996 Baldwin RL. On-pathway versus off-pathway folding intermediates Folding and Design. 1: R1-R8. PMID 9079355  1
1996 Rohl CA, Chakrabartty A, Baldwin RL. Helix propagation and N-cap propensities of the amino acids measured in alanine-based peptides in 40 volume percent trifluoroethanol. Protein Science : a Publication of the Protein Society. 5: 2623-37. PMID 8976571 DOI: 10.1002/pro.5560051225  1
1996 Baldwin RL. How Hofmeister ion interactions affect protein stability Biophysical Journal. 71: 2056-2063. PMID 8889180  1
1996 Loh SN, Rohl CA, Kiefhaber T, Baldwin RL. A general two-process model describes the hydrogen exchange behavior of RNase A in unfolding conditions. Proceedings of the National Academy of Sciences of the United States of America. 93: 1982-7. PMID 8700871 DOI: 10.1073/pnas.93.5.1982  1
1996 Jamin M, Baldwin RL. Refolding and unfolding kinetics of the equilibrium folding intermediate of apomyoglobin Nature Structural Biology. 3: 613-618. PMID 8673605 DOI: 10.1038/nsb0796-613  1
1996 Kiefhaber T, Baldwin RL. Hydrogen exchange and the unfolding pathway of ribonuclease A. Biophysical Chemistry. 59: 351-6. PMID 8672722 DOI: 10.1016/0301-4622(95)00142-5  1
1996 Padmanabhan S, York EJ, Stewart JM, Baldwin RL. Helix propensities of basic amino acids increase with the length of the side-chain Journal of Molecular Biology. 257: 726-734. PMID 8648636 DOI: 10.1006/jmbi.1996.0197  1
1996 Kay MS, Baldwin RL. Packing interactions in the apomyglobin folding intermediate Nature Structural Biology. 3: 439-445. PMID 8612074 DOI: 10.1038/nsb0596-439  1
1996 Baldwin RL. Why is protein folding so fast? Proceedings of the National Academy of Sciences of the United States of America. 93: 2627-2628. PMID 8610091 DOI: 10.1073/pnas.93.7.2627  1
1995 Scholtz JM, Barrick D, York EJ, Stewart JM, Baldwin RL. Urea unfolding of peptide helices as a model for interpreting protein unfolding. Proceedings of the National Academy of Sciences of the United States of America. 92: 185-9. PMID 7816813 DOI: 10.1073/pnas.92.1.185  1
1995 Loh SN, Kay MS, Baldwin RL. Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway Proceedings of the National Academy of Sciences of the United States of America. 92: 5446-5450. PMID 7777528 DOI: 10.1073/pnas.92.12.5446  1
1995 Kiefhaber T, Labhardt AM, Baldwin RL. Direct NMR evidence for an intermediate preceding the rate-limiting step in the unfolding of ribonuclease A. Nature. 375: 513-5. PMID 7777063 DOI: 10.1038/375513a0  1
1995 Chakrabartty A, Baldwin RL. Stability of α-helices Advances in Protein Chemistry. 46: 141-176. PMID 7771317  1
1995 Kiefhaber T, Baldwin RL. Kinetics of hydrogen bond breakage in the process of unfolding of ribonuclease A measured by pulsed hydrogen exchange. Proceedings of the National Academy of Sciences of the United States of America. 92: 2657-61. PMID 7708700 DOI: 10.1073/pnas.92.7.2657  1
1995 Baldwin RL. The nature of protein folding pathways: The classical versus the new view Journal of Biomolecular Nmr. 5: 103-109. PMID 7703696 DOI: 10.1007/BF00208801  1
1995 Udgaonkar JB, Baldwin RL. Nature of the early folding intermediate of ribonuclease A. Biochemistry. 34: 4088-96. PMID 7696273  1
1995 Doig AJ, Baldwin RL. N- and C-capping preferences for all 20 amino acids in α-helical peptides Protein Science. 4: 1325-1336. PMID 7670375  1
1995 Kiefhaber T, Baldwin RL. Intrinsic stability of individual alpha helices modulates structure and stability of the apomyoglobin molten globule form. Journal of Molecular Biology. 252: 122-32. PMID 7666424  1
1995 Baldwin RL. α-Helix formation by peptides of defined sequence Biophysical Chemistry. 55: 127-135. PMID 7632873 DOI: 10.1016/0301-4622(94)00146-B  1
1995 Huyghues-Despointes BMP, Klingler TM, Baldwin RL. Measuring the strenght of side-chain hydrogen bonds in peptide helices: The Gln·Asp (i, i + 4) interaction Biochemistry. 34: 13267-13271. PMID 7577910 DOI: 10.1021/bi00041a001  1
1994 Mayo SL, Baldwin RL. For the record. Science (New York, N.Y.). 263: 455. PMID 17754870 DOI: 10.1126/science.263.5146.455-a  1
1994 Baldwin RL. Matching speed and stability Nature. 369: 183-184. PMID 8183335 DOI: 10.1038/369183a0  1
1994 Baldwin RL. Finding intermediates in protein folding Bioessays. 16: 207-210. PMID 8166675  1
1994 Barrick D, Hughson FM, Baldwin RL. Molecular mechanisms of acid denaturation. The role of histidine residues in the partial unfolding of apomyoglobin. Journal of Molecular Biology. 237: 588-601. PMID 8158639 DOI: 10.1006/jmbi.1994.1257  1
1994 Doig AJ, Chakrabartty A, Klingler TM, Baldwin RL. Determination of free energies of N-capping in α-helices by modification of the Lifson-Roig helix-coil theory to include N- and C-capping Biochemistry. 33: 3396-3403. PMID 8136377  1
1994 Padmanabhan S, Baldwin RL. Helix-stabilizing interaction between tyrosine and leucine or valine when the spacing is i, i + 4 Journal of Molecular Biology. 241: 706-713. PMID 8071994 DOI: 10.1006/jmbi.1994.1545  1
1994 Chakrabartty A, Kortemme T, Baldwin RL. Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions. Protein Science : a Publication of the Protein Society. 3: 843-52. PMID 8061613 DOI: 10.1002/pro.5560030514  1
1994 Padmanabhan S, York EJ, Gera L, Stewart JM, Baldwin RL. 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 Biochemistry. 33: 8604-8609. PMID 8031795  1
1994 Rohl CA, Baldwin RL. Exchange kinetics of individual amide protons in 15N-labeled helical peptides measured by isotope-edited NMR. Biochemistry. 33: 7760-7. PMID 8011641  1
1994 Padmanabhan S, Baldwin RL. Tests for helix-stabilizing interactions between various nonpolar side chains in alanine-based peptides Protein Science. 3: 1992-1997. PMID 7703846  1
1994 Mayo SL, Baldwin RL. For the record [5] Science. 263: 455.  1
1993 Chakrabartty A, Kortemme T, Padmanabhan S, Baldwin RL. Aromatic side-chain contribution to far-ultraviolet circular dichroism of helical peptides and its effect on measurement of helix propensities. Biochemistry. 32: 5560-5. PMID 8504077  1
1993 Scholtz JM, Baldwin RL. Perchlorate-induced denaturation of ribonuclease A: investigation of possible folding intermediates. Biochemistry. 32: 4604-8. PMID 8387338  1
1993 Mayo SL, Baldwin RL. Guanidinium chloride induction of partial unfolding in amide proton exchange in RNase A. Science (New York, N.Y.). 262: 873-6. PMID 8235609  1
1992 Schultz DA, Schmid FX, Baldwin RL. Cis proline mutants of ribonuclease A. II. Elimination of the slow-folding forms by mutation. Protein Science : a Publication of the Protein Society. 1: 917-24. PMID 1304376 DOI: 10.1002/pro.5560010710  1
1991 Hughson FM, Barrick D, Baldwin RL. Probing the stability of a partly folded apomyoglobin intermediate by site-directed mutagenesis. Biochemistry. 30: 4113-8. PMID 2021603  1
1991 Scholtz JM, Marqusee S, Baldwin RL, York EJ, Stewart JM, Santoro M, Bolen DW. Calorimetric determination of the enthalpy change for the alpha-helix to coil transition of an alanine peptide in water. Proceedings of the National Academy of Sciences of the United States of America. 88: 2854-8. PMID 2011594  1
1990 Padmanabhan S, Marqusee S, Ridgeway T, Laue TM, Baldwin RL. Relative helix-forming tendencies of nonpolar amino acids. Nature. 344: 268-70. PMID 2314462 DOI: 10.1038/344268a0  1
1990 Udgaonkar JB, Baldwin RL. Early folding intermediate of ribonuclease A. Proceedings of the National Academy of Sciences of the United States of America. 87: 8197-201. PMID 2236032  1
1990 Hughson FM, Wright PE, Baldwin RL. Structural characterization of a partly folded apomyoglobin intermediate. Science (New York, N.Y.). 249: 1544-8. PMID 2218495  1
1990 Kim PS, Baldwin RL. Intermediates in the folding reactions of small proteins. Annual Review of Biochemistry. 59: 631-60. PMID 2197986 DOI: 10.1146/annurev.bi.59.070190.003215  1
1989 Hughson FM, Baldwin RL. Use of site-directed mutagenesis to destabilize native apomyoglobin relative to folding intermediates. Biochemistry. 28: 4415-22. PMID 2765493  1
1989 Marqusee S, Robbins VH, Baldwin RL. Unusually stable helix formation in short alanine-based peptides. Proceedings of the National Academy of Sciences of the United States of America. 86: 5286-90. PMID 2748584  1
1988 Udgaonkar JB, Baldwin RL. NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A. Nature. 335: 694-9. PMID 2845278 DOI: 10.1038/335694a0  1
1987 Shoemaker KR, Kim PS, York EJ, Stewart JM, Baldwin RL. Tests of the helix dipole model for stabilization of alpha-helices. Nature. 326: 563-7. PMID 3561498 DOI: 10.1038/326563a0  1
1987 Shoemaker KR, Fairman R, Kim PS, York EJ, Stewart JM, Baldwin RL. The C-peptide helix from ribonuclease A considered as an autonomous folding unit. Cold Spring Harbor Symposia On Quantitative Biology. 52: 391-8. PMID 3454268  1
1987 Marqusee S, Baldwin RL. Helix stabilization by Glu-...Lys+ salt bridges in short peptides of de novo design. Proceedings of the National Academy of Sciences of the United States of America. 84: 8898-902. PMID 3122208  1
1986 Loftus D, Gbenle GO, Kim PS, Baldwin RL. Effects of denaturants on amide proton exchange rates: a test for structure in protein fragments and folding intermediates. Biochemistry. 25: 1428-36. PMID 3964684  1
1985 Shoemaker KR, Kim PS, Brems DN, Marqusee S, York EJ, Chaiken IM, Stewart JM, Baldwin RL. Nature of the charged-group effect on the stability of the C-peptide helix. Proceedings of the National Academy of Sciences of the United States of America. 82: 2349-53. PMID 3857585 DOI: 10.1073/pnas.82.8.2349  1
1984 Kim PS, Baldwin RL. A helix stop signal in the isolated S-peptide of ribonuclease A. Nature. 307: 329-34. PMID 6694731  1
1984 Schmid FX, Buonocore MH, Baldwin RL. Tests of the simple model of Lin and Brandts for the folding kinetics of ribonuclease A. Biochemistry. 23: 3389-94. PMID 6466645  1
1983 Kuwajima K, Kim PS, Baldwin RL. Strategy for trapping intermediates in the folding of ribonuclease and for using 1H-nmr to determine their structures. Biopolymers. 22: 59-67. PMID 6673773 DOI: 10.1002/bip.360220111  1
1982 Kim PS, Bierzynski A, Baldwin RL. A competing salt-bridge suppresses helix formation by the isolated C-peptide carboxylate of ribonuclease A. Journal of Molecular Biology. 162: 187-99. PMID 6296404  1
1982 Kim PS, Baldwin RL. Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. Annual Review of Biochemistry. 51: 459-89. PMID 6287919 DOI: 10.1146/annurev.bi.51.070182.002331  1
1982 Bierzynski A, Kim PS, Baldwin RL. A salt bridge stabilizes the helix formed by isolated C-peptide of RNase A. Proceedings of the National Academy of Sciences of the United States of America. 79: 2470-4. PMID 6283528  1
1982 Kim PS, Baldwin RL. Influence of charge on the rate of amide proton exchange. Biochemistry. 21: 1-5. PMID 6174148  1
1980 Kim PS, Cook KH, Baldwin RL. Studies of the intermediates in the folding of ribonuclease a. Biophysical Journal. 32: 427-8. PMID 19431380  1
1980 Kim PS, Baldwin RL. Structural intermediates trapped during the folding of ribonuclease A by amide proton exchange. Biochemistry. 19: 6124-9. PMID 6258629  1
1979 Cook KH, Schmid FX, Baldwin RL. Role of proline isomerization in folding of ribonuclease A at low temperatures. Proceedings of the National Academy of Sciences of the United States of America. 76: 6157-61. PMID 293712  1
1979 Schmid FX, Baldwin RL. The rate of interconversion between the two unfolded forms of ribonuclease A does not depend on guanidinium chloride concentration. Journal of Molecular Biology. 133: 285-7. PMID 231661  1
1979 Schmid FX, Baldwin RL. Detection of an early intermediate in the folding of ribonuclease A by protection of amide protons against exchange. Journal of Molecular Biology. 135: 199-215. PMID 43397  1
1979 Hagerman PJ, Schmid FX, Baldwin RL. Refolding behavior of a kinetic intermediate observed in the low pH unfolding of ribonuclease A. Biochemistry. 18: 293-7. PMID 33695  1
1978 Schmid FX, Baldwin RL. Acid catalysis of the formation of the slow-folding species of RNase A: evidence that the reaction is proline isomerization. Proceedings of the National Academy of Sciences of the United States of America. 75: 4764-8. PMID 283390  1
1962 WAKE RG, BALDWIN RL. Physical studies on the replication of DNA in vitro. Journal of Molecular Biology. 5: 201-16. PMID 13998372  1
1961 WAKE RG, BALDWIN RL. Analysis of casein fractions by zone electrophoresis in concentrated urea. Biochimica Et Biophysica Acta. 47: 225-39. PMID 13782592  1
1958 O'DONNELL IJ, BALDWIN RL, WILLIAMS JW. Correlation of the N=a reaction of thyroglobulin with the type of breakdown produced by papain. Biochimica Et Biophysica Acta. 28: 294-308. PMID 13535726  0.4
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