| Year |
Citation |
Score |
| 2017 |
Baldwin RL. Clash between energy landscape theory and foldon-dependent protein folding. Proceedings of the National Academy of Sciences of the United States of America. PMID 28747526 DOI: 10.1073/Pnas.1709133114 |
0.378 |
|
| 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 |
0.349 |
|
| 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 |
0.316 |
|
| 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 |
0.311 |
|
| 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 |
0.375 |
|
| 2011 |
Baldwin RL. Early days of protein hydrogen exchange: 1954-1972. Proteins. 79: 2021-6. PMID 21557321 DOI: 10.1002/Prot.23039 |
0.386 |
|
| 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 |
0.419 |
|
| 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 |
0.383 |
|
| 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 |
0.435 |
|
| 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 |
0.385 |
|
| 2009 |
Baldwin RL. In memoriam: Reflections on Fred Richards (1925–2009) Protein Science. 18: 682-685. DOI: 10.1002/Pro.81 |
0.368 |
|
| 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 |
0.435 |
|
| 2008 |
Baldwin RL. Structure and mechanism in protein science. A guide to enzyme catalysis and protein folding, by A. Fersht. 1999. New York: Freeman. 631 pp. $67.95 (hardcover) Protein Science. 9: 207-207. DOI: 10.1110/Ps.9.1.207 |
0.312 |
|
| 2007 |
Baldwin RL. Energetics of protein folding. Journal of Molecular Biology. 371: 283-301. PMID 17582437 DOI: 10.1016/J.Jmb.2007.05.078 |
0.427 |
|
| 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 |
0.433 |
|
| 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 |
0.377 |
|
| 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 |
0.33 |
|
| 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 |
0.435 |
|
| 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 |
0.382 |
|
| 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 |
0.403 |
|
| 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 |
0.382 |
|
| 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 |
0.427 |
|
| 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 |
0.413 |
|
| 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 |
0.437 |
|
| 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 |
0.319 |
|
| 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 |
0.387 |
|
| 2002 |
Baldwin RL. Making a network of hydrophobic clusters. Science (New York, N.Y.). 295: 1657-8. PMID 11872825 DOI: 10.1126/Science.1069893 |
0.316 |
|
| 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 |
0.39 |
|
| 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 |
0.345 |
|
| 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 |
0.454 |
|
| 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 |
0.416 |
|
| 2001 |
Luo Y, Baldwin RL. How Ala-->Gly mutations in different helices affect the stability of the apomyoglobin molten globule. Biochemistry. 40: 5283-9. PMID 11318652 DOI: 10.1021/Bi010122J |
0.367 |
|
| 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 |
0.601 |
|
| 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 DOI: 10.1073/Pnas.200343197 |
0.436 |
|
| 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 DOI: 10.1110/Ps.9.7.1340 |
0.42 |
|
| 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 |
0.4 |
|
| 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 |
0.399 |
|
| 1999 |
Baldwin RL. Protein folding from 1961 to 1982 Nature Structural Biology. 6: 814-817. PMID 10467090 DOI: 10.1038/12268 |
0.384 |
|
| 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 |
0.376 |
|
| 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 |
0.398 |
|
| 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 |
0.39 |
|
| 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 |
0.43 |
|
| 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 |
0.399 |
|
| 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 |
0.436 |
|
| 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 |
0.397 |
|
| 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 |
0.371 |
|
| 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 |
0.379 |
|
| 1998 |
Laurents DV, Baldwin RL. Protein folding: Matching theory and experiment Biophysical Journal. 75: 428-434. PMID 9649403 DOI: 10.1016/S0006-3495(98)77530-7 |
0.394 |
|
| 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 |
0.447 |
|
| 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 |
0.37 |
|
| 1998 |
Geierstanger B, Jamin M, Volkman BF, Baldwin RL. Protonation Behavior of Histidine 24 and Histidine 119 in Forming the pH 4 Folding Intermediate of Apomyoglobin Biochemistry. 37: 4254-4265. PMID 9521748 DOI: 10.1021/Bi972516+ |
0.4 |
|
| 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 |
0.391 |
|
| 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 |
0.444 |
|
| 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 |
0.416 |
|
| 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 |
0.385 |
|
| 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 |
0.445 |
|
| 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 |
0.438 |
|
| 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 |
0.417 |
|
| 1996 |
Baldwin RL. On-pathway versus off-pathway folding intermediates Folding and Design. 1: R1-R8. PMID 9079355 DOI: 10.1016/S1359-0278(96)00003-X |
0.368 |
|
| 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 |
0.353 |
|
| 1996 |
Baldwin RL. How Hofmeister ion interactions affect protein stability Biophysical Journal. 71: 2056-2063. PMID 8889180 DOI: 10.1016/S0006-3495(96)79404-3 |
0.323 |
|
| 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 |
0.752 |
|
| 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 |
0.403 |
|
| 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 |
0.758 |
|
| 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 |
0.331 |
|
| 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 |
0.416 |
|
| 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 |
0.439 |
|
| 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 |
0.749 |
|
| 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 |
0.426 |
|
| 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 |
0.738 |
|
| 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 |
0.754 |
|
| 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 |
0.429 |
|
| 1995 |
Udgaonkar JB, Baldwin RL. Nature of the early folding intermediate of ribonuclease A. Biochemistry. 34: 4088-96. PMID 7696273 DOI: 10.1021/Bi00012A027 |
0.566 |
|
| 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 DOI: 10.1002/Pro.5560040708 |
0.383 |
|
| 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 DOI: 10.1006/Jmbi.1995.0479 |
0.763 |
|
| 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 |
0.39 |
|
| 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 |
0.411 |
|
| 1995 |
Chakrabartty A, Baldwin RL. Stability Of Alpha -Helices Advances in Protein Chemistry. 46: 141-176. DOI: 10.1016/S0065-3233(08)60334-4 |
0.44 |
|
| 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 |
0.468 |
|
| 1994 |
Baldwin RL. Finding intermediates in protein folding Bioessays. 16: 207-210. PMID 8166675 DOI: 10.1002/Bies.950160312 |
0.343 |
|
| 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 |
0.757 |
|
| 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 DOI: 10.1021/Bi00177A033 |
0.363 |
|
| 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 |
0.405 |
|
| 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 |
0.456 |
|
| 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 DOI: 10.1021/Bi00194A027 |
0.397 |
|
| 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 DOI: 10.1021/Bi00191A003 |
0.43 |
|
| 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 DOI: 10.1002/Pro.5560031111 |
0.412 |
|
| 1994 |
Mayo SL, Baldwin RL. For the record [5] Science. 263: 455. |
0.468 |
|
| 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 DOI: 10.1021/Bi00072A010 |
0.422 |
|
| 1993 |
Barrick D, Baldwin RL. Three-state analysis of sperm whale apomyoglobin folding Biochemistry. 32: 3790-3796. PMID 8466917 DOI: 10.1021/Bi00065A035 |
0.602 |
|
| 1993 |
Armstrong KM, Fairman R, Baldwin RL. The (i, i + 4) Phe-His interaction studied in an alanine-based alpha-helix. Journal of Molecular Biology. 230: 284-91. PMID 8450542 DOI: 10.1006/Jmbi.1993.1142 |
0.65 |
|
| 1993 |
Huyghues-Despointes BM, Scholtz JM, Baldwin RL. Helical peptides with three pairs of Asp-Arg and Glu-Arg residues in different orientations and spacings. Protein Science : a Publication of the Protein Society. 2: 80-5. PMID 8443591 DOI: 10.1002/Pro.5560020108 |
0.665 |
|
| 1993 |
Scholtz JM, Baldwin RL. Perchlorate-induced denaturation of ribonuclease A: investigation of possible folding intermediates. Biochemistry. 32: 4604-8. PMID 8387338 |
0.579 |
|
| 1993 |
Scholtz JM, Qian H, Robbins VH, Baldwin RL. The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide. Biochemistry. 32: 9668-76. PMID 8373771 DOI: 10.1021/Bi00088A019 |
0.691 |
|
| 1993 |
Barrick D, Baldwin RL. The molten globule intermediate of apomyoglobin and the process of protein folding Protein Science. 2: 869-876. PMID 8318892 DOI: 10.1002/Pro.5560020601 |
0.632 |
|
| 1993 |
Huyghues-Despointes BM, Scholtz JM, Baldwin RL. Effect of a single aspartate on helix stability at different positions in a neutral alanine-based peptide. Protein Science : a Publication of the Protein Society. 2: 1604-11. PMID 8251935 DOI: 10.1002/Pro.5560021006 |
0.669 |
|
| 1993 |
Armstrong KM, Baldwin RL. Charged histidine affects alpha-helix stability at all positions in the helix by interacting with the backbone charges. Proceedings of the National Academy of Sciences of the United States of America. 90: 11337-40. PMID 8248249 DOI: 10.1073/Pnas.90.23.11337 |
0.377 |
|
| 1993 |
Chakrabartty A, Doig AJ, Baldwin RL. Helix capping propensities in peptides parallel those in proteins Proceedings of the National Academy of Sciences of the United States of America. 90: 11332-11336. PMID 8248248 DOI: 10.1073/Pnas.90.23.11332 |
0.39 |
|
| 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 DOI: 10.1126/Science.8235609 |
0.643 |
|
| 1993 |
Laurents DV, Doig AJ, Schultz DA, Baldwin RL. Characterization of a ribonuclease S refolding intermediate Philosophical Transactions of the Royal Society A. 345: 131-140. DOI: 10.1098/Rsta.1993.0124 |
0.353 |
|
| 1993 |
Baldwin RL. Intermediates in protein folding Protein Engineering. 6: 5-5. DOI: 10.1093/Protein/6.Supplement.5 |
0.343 |
|
| 1993 |
Baldwin RL. Pulsed H/D-exchange studies of folding intermediates Current Opinion in Structural Biology. 3: 84-91. DOI: 10.1016/0959-440X(93)90206-Z |
0.365 |
|
| 1992 |
Scholtz JM, Baldwin RL. The mechanism of alpha-helix formation by peptides. Annual Review of Biophysics and Biomolecular Structure. 21: 95-118. PMID 1525475 DOI: 10.1146/Annurev.Bb.21.060192.000523 |
0.658 |
|
| 1992 |
Baldwin RL, Muller N. Relation between the convergence temperatures Th* and Ts* in protein unfolding. Proceedings of the National Academy of Sciences of the United States of America. 89: 7110-7113. PMID 1496007 DOI: 10.1073/Pnas.89.15.7110 |
0.34 |
|
| 1992 |
Schultz DA, Baldwin RL. Cis proline mutants of ribonuclease A. I. Thermal stability. Protein Science. 1: 910-916. PMID 1338975 DOI: 10.1002/Pro.5560010709 |
0.398 |
|
| 1992 |
Rohl CA, Scholtz JM, York EJ, Stewart JM, Baldwin RL. Kinetics of amide proton exchange in helical peptides of varying chain lengths. Interpretation by the Lifson-Roig equation. Biochemistry. 31: 1263-9. PMID 1310608 DOI: 10.1021/Bi00120A001 |
0.668 |
|
| 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 |
0.673 |
|
| 1991 |
Chakrabartty A, Schellman JA, Baldwin RL. Large differences in the helix propensities of alanine and glycine. Nature. 351: 586-8. PMID 2046766 DOI: 10.1038/351586A0 |
0.418 |
|
| 1991 |
Strehlow KG, Robertson AD, Baldwin RL. Proline for alanine substitutions in the C-peptide helix of ribonuclease A Biochemistry. 30: 5810-5814. PMID 2043620 DOI: 10.1021/Bi00237A026 |
0.597 |
|
| 1991 |
Padmanabhan S, Baldwin RL. Straight-chain non-polar amino acids are good helix-formers in water☆ Journal of Molecular Biology. 219: 135-137. PMID 2038048 DOI: 10.1016/0022-2836(91)90553-I |
0.367 |
|
| 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 DOI: 10.1021/Bi00231A001 |
0.679 |
|
| 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 DOI: 10.1073/Pnas.88.7.2854 |
0.745 |
|
| 1991 |
Fairman R, Armstrong KM, Shoemaker KR, York EJ, Stewart JM, Baldwin RL. Position effect on apparent helical propensities in the C-peptide helix. Journal of Molecular Biology. 221: 1395-401. PMID 1942058 DOI: 10.1016/0022-2836(91)90940-8 |
0.658 |
|
| 1991 |
Scholtz JM, Qian H, York EJ, Stewart JM, Baldwin RL. Parameters of helix-coil transition theory for alanine-based peptides of varying chain lengths in water. Biopolymers. 31: 1463-70. PMID 1814498 DOI: 10.1002/Bip.360311304 |
0.703 |
|
| 1991 |
Scholtz JM, York EJ, Stewart JM, Baldwin RL. A neutral, water-soluble, .alpha.-helical peptide: the effect of ionic strength on the helix-coil equilibrium Journal of the American Chemical Society. 113: 5102-5104. DOI: 10.1021/Ja00013A079 |
0.622 |
|
| 1991 |
Baldwin RL, Roder H. Characterizing protein folding intermediates Current Biology. 1: 218-220. DOI: 10.1016/0960-9822(91)90061-Z |
0.346 |
|
| 1990 |
Shoemaker KR, Fairman R, Schultz DA, Robertson AD, York EJ, Stewart JM, Baldwin RL. Side-chain interactions in the C-peptide helix: Phe 8 ... His 12+. Biopolymers. 29: 1-11. PMID 2328280 DOI: 10.1002/Bip.360290104 |
0.734 |
|
| 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 |
0.616 |
|
| 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 DOI: 10.1073/Pnas.87.21.8197 |
0.595 |
|
| 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 DOI: 10.1126/Science.2218495 |
0.69 |
|
| 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 |
0.553 |
|
| 1990 |
Fairman R, Shoemaker KR, York EJ, Stewart JM, Baldwin RL. The Glu 2- ... Arg 10+ side-chain interaction in the C-peptide helix of ribonuclease A. Biophysical Chemistry. 37: 107-19. PMID 1981024 DOI: 10.1016/0301-4622(90)88012-H |
0.69 |
|
| 1990 |
Baldwin RL. Pieces of the folding puzzle Nature. 346: 409-410. DOI: 10.1038/346409A0 |
0.352 |
|
| 1989 |
Osterhout JJ, Baldwin RL, York EJ, Stewart JM, Dyson HJ, Wright PE. 1H NMR studies of the solution conformations of an analogue of the C-peptide of ribonuclease A. Biochemistry. 28: 7059-64. PMID 2819049 DOI: 10.1021/Bi00443A042 |
0.41 |
|
| 1989 |
Hughson FM, Baldwin RL. Use of site-directed mutagenesis to destabilize native apomyoglobin relative to folding intermediates. Biochemistry. 28: 4415-22. PMID 2765493 DOI: 10.1021/Bi00436A044 |
0.691 |
|
| 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 DOI: 10.1073/Pnas.86.14.5286 |
0.647 |
|
| 1989 |
Fairman R, Shoemaker KR, York EJ, Stewart JM, Baldwin RL. Further studies of the helix dipole model: effects of a free alpha-NH3+ or alpha-COO- group on helix stability. Proteins. 5: 1-7. PMID 2748569 DOI: 10.1002/Prot.340050102 |
0.64 |
|
| 1989 |
Strehlow KG, Baldwin RL. Effect of the substitution Ala----Gly at each of five residue positions in the C-peptide helix. Biochemistry. 28: 2130-2133. PMID 2719948 DOI: 10.1021/Bi00431A025 |
0.431 |
|
| 1989 |
Baldwin RL. How does protein folding get started? Trends in Biochemical Sciences. 14: 291-294. PMID 2672452 DOI: 10.1016/0968-0004(89)90067-4 |
0.355 |
|
| 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 |
0.618 |
|
| 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 |
0.544 |
|
| 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 DOI: 10.1101/Sqb.1987.052.01.045 |
0.699 |
|
| 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 DOI: 10.1073/Pnas.84.24.8898 |
0.656 |
|
| 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 DOI: 10.1021/Bi00354A036 |
0.537 |
|
| 1986 |
Utiyama H, Baldwin RL. Kinetic mechanisms of protein folding. Methods in Enzymology. 131: 51-70. PMID 3773771 DOI: 10.1016/0076-6879(86)31034-6 |
0.344 |
|
| 1986 |
Baldwin RL. Protein folding: Introductory comments Methods in Enzymology. 3-4. PMID 3773763 DOI: 10.1016/0076-6879(86)31032-2 |
0.329 |
|
| 1986 |
Baldwin RL. Temperature dependence of the hydrophobic interaction in protein folding Proceedings of the National Academy of Sciences of the United States of America. 83: 8069-8072. PMID 3464944 DOI: 10.1073/Pnas.83.21.8069 |
0.331 |
|
| 1986 |
Mitchinson C, Baldwin RL. The design and production of semisynthetic ribonucleases with increased thermostability by incorporation of S-peptide analogues with enhanced helical stability. Proteins. 1: 23-33. PMID 3449849 DOI: 10.1002/Prot.340010106 |
0.421 |
|
| 1986 |
Baldwin RL. Seeding protein folding Trends in Biochemical Sciences. 11: 6-9. DOI: 10.1016/0968-0004(86)90219-7 |
0.39 |
|
| 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 |
0.721 |
|
| 1985 |
Brems DN, Baldwin RL. Protection of amide protons in folding intermediates of ribonuclease A measured by pH-pulse exchange curves. Biochemistry. 24: 1689-1693. PMID 2988608 DOI: 10.1021/Bi00328A018 |
0.398 |
|
| 1984 |
Kim PS, Baldwin RL. A helix stop signal in the isolated S-peptide of ribonuclease A. Nature. 307: 329-34. PMID 6694731 DOI: 10.1038/307329A0 |
0.546 |
|
| 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 DOI: 10.1021/Bi00310A002 |
0.652 |
|
| 1984 |
Brems DN, Baldwin RL. Amide proton exchange used to monitor the formation of a stable α-helix by residues 3 to 13 during folding of ribonuclease S Journal of Molecular Biology. 180: 1141-1156. PMID 6098689 DOI: 10.1016/0022-2836(84)90274-2 |
0.453 |
|
| 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 |
0.588 |
|
| 1983 |
Labhardt AM, Ridge JA, Lindquist RN, Baldwin RL. Measurement of the refolding combination reaction between S-peptide and S-protein. Biochemistry. 22: 321-327. PMID 6402007 DOI: 10.1021/Bi00271A014 |
0.397 |
|
| 1983 |
Kuwajima K, Baldwin RL. Exchange behavior of the H-bonded amide protons in the 3 to 13 helix of ribonuclease S* Journal of Molecular Biology. 169: 299-323. PMID 6312052 DOI: 10.1016/S0022-2836(83)80185-5 |
0.409 |
|
| 1983 |
Kuwajima K, Baldwin RL. Nature and locations of the most slowly exchanging peptide NH protons in residues 1 to 19 of ribonuclease S Journal of Molecular Biology. 169: 281-297. PMID 6312051 DOI: 10.1016/S0022-2836(83)80184-3 |
0.432 |
|
| 1982 |
Bierzynski A, Baldwin RL. Local secondary structure in ribonuclease A denatured by guanidine · HCl near 1 °C Journal of Molecular Biology. 162: 173-186. PMID 7154094 DOI: 10.1016/0022-2836(82)90167-X |
0.46 |
|
| 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 DOI: 10.1016/0022-2836(82)90168-1 |
0.56 |
|
| 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 |
0.513 |
|
| 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 DOI: 10.1073/Pnas.79.8.2470 |
0.609 |
|
| 1982 |
Kim PS, Baldwin RL. Influence of charge on the rate of amide proton exchange. Biochemistry. 21: 1-5. PMID 6174148 DOI: 10.1021/Bi00530A001 |
0.455 |
|
| 1982 |
Kim P, Baldwin R. Corrections - Influence of Charge on the Rate of Amide Proton Exchange Biochemistry. 21: 3036-3036. DOI: 10.1021/Bi00541A605 |
0.455 |
|
| 1981 |
Jullien M, Baldwin RL. The role of proline residues in the folding kinetics of the bovine pancreatic trypsin inhibitor derivative RCAM(14-38). Journal of Molecular Biology. 145: 265-280. PMID 7265200 DOI: 10.1016/0022-2836(81)90343-0 |
0.411 |
|
| 1981 |
Ridge JA, Baldwin RL, Labhardt AM. Nature of the fast and slow refolding reactions of iron(III) cytochrome c. Biochemistry. 20: 1622-1630. PMID 6261802 DOI: 10.1021/Bi00509A033 |
0.323 |
|
| 1980 |
Kim PS, Cook KH, Baldwin RL. Studies of the intermediates in the folding of ribonuclease a. Biophysical Journal. 32: 427-8. PMID 19431380 DOI: 10.1016/S0006-3495(80)84968-X |
0.531 |
|
| 1980 |
Kim PS, Baldwin RL. Structural intermediates trapped during the folding of ribonuclease A by amide proton exchange. Biochemistry. 19: 6124-9. PMID 6258629 DOI: 10.1021/Bi00567A027 |
0.572 |
|
| 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 DOI: 10.1073/Pnas.76.12.6157 |
0.689 |
|
| 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 DOI: 10.1016/0022-2836(79)90536-9 |
0.667 |
|
| 1979 |
Labhardt AM, Baldwin RL. 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. Journal of Molecular Biology. 135: 245-254. PMID 43399 DOI: 10.1016/0022-2836(79)90350-4 |
0.406 |
|
| 1979 |
Labhardt AM, Baldwin RL. 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. Journal of Molecular Biology. 135: 231-244. PMID 43398 DOI: 10.1016/0022-2836(79)90349-8 |
0.428 |
|
| 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 DOI: 10.1016/0022-2836(79)90347-4 |
0.714 |
|
| 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 DOI: 10.1021/Bi00569A009 |
0.668 |
|
| 1978 |
Nall BT, Garel JR, Baldwin RL. Test of the extended two-state model for the kinetic intermediates observed in the folding transition of ribonuclease A Journal of Molecular Biology. 118: 317-330. PMID 633363 DOI: 10.1016/0022-2836(78)90231-0 |
0.406 |
|
| 1978 |
Blum AD, Smallcombe SH, Baldwin RL. Nuclear magnetic resonance evidence for a structural intermediate at an early stage in the refolding of ribonuclease A. Journal of Molecular Biology. 118: 305-316. PMID 633362 DOI: 10.1016/0022-2836(78)90230-9 |
0.403 |
|
| 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 DOI: 10.1073/Pnas.75.10.4764 |
0.693 |
|
| 1978 |
Baldwin RL. The pathway of protein folding Trends in Biochemical Sciences. 3: 66-68. DOI: 10.1016/S0968-0004(78)94092-6 |
0.342 |
|
| 1978 |
Tsong TY, Baldwin RL. Effects of solvent viscosity and different guanidine salts on the kinetics of ribonuclease A chain folding Biopolymers. 17: 1669-1678. DOI: 10.1002/Bip.1978.360170705 |
0.366 |
|
| 1977 |
Christiansen C, Baldwin RL. Catalysis of DNA reassociation by the Escherichia coli DNA binding protein: A polyamine-dependent reaction☆ Journal of Molecular Biology. 115: 441-454. PMID 22760 DOI: 10.1016/0022-2836(77)90164-4 |
0.331 |
|
| 1977 |
Schreier AA, Baldwin RL. Mechanism of dissociation of S-peptide from ribonuclease S. Biochemistry. 16: 4203-9. PMID 20135 DOI: 10.1021/Bi00638A012 |
0.326 |
|
| 1977 |
Nall BT, Baldwin RL. Thermal unfolding transition of ribonuclease A measured by 2′-CMP binding Biochemistry. 16: 3572-3576. PMID 19055 DOI: 10.1021/Bi00635A011 |
0.334 |
|
| 1976 |
Garel JR, Nall BT, Baldwin RL. Guanidine unfolded state of ribonuclease A contains both fast and slow refolding species Proceedings of the National Academy of Sciences of the United States of America. 73: 1853-1857. PMID 1064858 DOI: 10.1073/Pnas.73.6.1853 |
0.368 |
|
| 1976 |
Schreier AA, Baldwin RL. Concentration-dependent hydrogen exchange kinetics of 3H-labeled S-peptide in ribonuclease S. Journal of Molecular Biology. 105: 409-26. PMID 9516 DOI: 10.1016/0022-2836(76)90101-7 |
0.424 |
|
| 1976 |
Hagerman PJ, Baldwin RL. A quantitative treatment of the kinetics of the folding transition of ribonuclease A Biochemistry. 15: 1462-1473. PMID 4087 DOI: 10.1021/Bi00652A017 |
0.34 |
|
| 1975 |
Baldwin RL. Intermediates in Protein Folding Reactions and the Mechanism of Protein Folding Annual Review of Biochemistry. 44: 453-475. PMID 1094916 DOI: 10.1146/Annurev.Bi.44.070175.002321 |
0.349 |
|
| 1975 |
Garel J, Baldwin RL. A physical difference between the fast- and slow-refolding forms of nitrotyrosyl ribonuclease A: the pK values of the nitrotyrosyl groups. Journal of Molecular Biology. 94: 621-632. PMID 241857 DOI: 10.1016/0022-2836(75)90326-5 |
0.33 |
|
| 1975 |
Garel J, Baldwin RL. The heat-unfolded state of ribonuclease A is an equilibrium mixture of fast and slow refolding species. Journal of Molecular Biology. 94: 611-620. PMID 241856 DOI: 10.1016/0022-2836(75)90325-3 |
0.349 |
|
| 1973 |
Garel J, Baldwin RL. Both the Fast and Slow Refolding Reactions of Ribonuclease A Yield Native Enzyme Proceedings of the National Academy of Sciences of the United States of America. 70: 3347-3351. PMID 4519627 DOI: 10.1073/Pnas.70.12.3347 |
0.325 |
|
| 1972 |
Tsong TY, Baldwin RL, McPhie P, Elson EL. A sequential model of nucleation-dependent protein folding: Kinetic studies of ribonuclease A Journal of Molecular Biology. 63: 453-469. PMID 5014928 DOI: 10.1016/0022-2836(72)90440-8 |
0.608 |
|
| 1972 |
Tsong TY, Baldwin RL. Kinetic evidence for intermediate states in the unfolding of ribonuclease A. II. Kinetics of exposure to solvent of a specific dinitrophenyl group. Journal of Molecular Biology. 69: 149-53. PMID 4672199 DOI: 10.1016/0022-2836(72)90030-7 |
0.33 |
|
| 1972 |
Tsong TY, Baldwin RL. Kinetic evidence for intermediate states in the unfolding of chymotrypsinogen A. Journal of Molecular Biology. 69: 145-8. PMID 4672198 DOI: 10.1016/0022-2836(72)90029-0 |
0.362 |
|
| 1972 |
Tsong TY, Baldwin RL, Elson EL. Properties of the refolding and unfolding reactions of ribonuclease A Proceedings of the National Academy of Sciences of the United States of America. 69: 1809-1812. PMID 4505658 DOI: 10.1073/Pnas.69.7.1809 |
0.59 |
|
| 1971 |
Tsong TY, Baldwin RL, Elson EL. The sequential unfolding of ribonuclease A: detection of a fast initial phase in the kinetics of unfolding Proceedings of the National Academy of Sciences of the United States of America. 68: 2712-2715. PMID 5288248 DOI: 10.1073/Pnas.68.11.2712 |
0.593 |
|
| 1970 |
Elson EL, Scheffler IE, Baldwin RL. Helix formation by d(TA) oligomers. III. Electrostatic effects Journal of Molecular Biology. 54: 401-415. PMID 5492017 DOI: 10.1016/0022-2836(70)90118-X |
0.573 |
|
| 1970 |
Scheffler IE, Elson EL, Baldwin RL. Helix formation by d(TA) oligomers. II. Analysis of the helix-coil transitions of linear and circular oligomers Journal of Molecular Biology. 48: 145-171. PMID 5448587 DOI: 10.1016/0022-2836(70)90225-1 |
0.592 |
|
| 1968 |
Scheffler IE, Elson EL, Baldwin RL. Helix Formation by dAT oligomers. I. Hairpin and straight-chain helices Journal of Molecular Biology. 36: 291-304. PMID 5760542 DOI: 10.1016/0022-2836(68)90156-3 |
0.571 |
|
| 1965 |
SPATZ H, BALDWIN RL. STUDY OF THE FOLDING OF THE DAT COPOLYMER BY KINETIC MEASUREMENTS OF MELTING. Journal of Molecular Biology. 11: 213-22. PMID 14290341 DOI: 10.1016/S0022-2836(65)80052-3 |
0.33 |
|
| 1964 |
Inman RB, Baldwin RL. Helix--Random Coil Transitions In Dna Homopolymer Pairs. Journal of Molecular Biology. 8: 452-469. PMID 14153518 DOI: 10.1016/S0022-2836(64)80003-6 |
0.352 |
|
| 1963 |
BALDWIN RL, SHOOTER EM. THE ALKALINE TRANSITION OF BU-CONTAINING DNA AND ITS BEARING ON THE REPLICATION OF DNA. Journal of Molecular Biology. 7: 511-26. PMID 14079590 DOI: 10.1016/S0022-2836(63)80098-4 |
0.532 |
|
| 1963 |
CHAMBERLIN M, BALDWIN RL, BERG P. AN ENZYMICALLY SYNTHESIZED RNA OF ALTERNATING BASE SEQUENCE: PHYSICAL Journal of Molecular Biology. 7: 334-349. PMID 14066612 DOI: 10.1016/S0022-2836(63)80028-5 |
0.312 |
|
| 1962 |
WAKE RG, BALDWIN RL. Physical studies on the replication of DNA in vitro. Journal of Molecular Biology. 5: 201-16. PMID 13998372 DOI: 10.1016/S0022-2836(62)80084-9 |
0.517 |
|
| 1962 |
Inman RB, Baldwin RL. Helix-random coil transitions in synthetic DNAs of alternating sequence Journal of Molecular Biology. 5: 172-184. PMID 13956560 DOI: 10.1016/S0022-2836(62)80082-5 |
0.306 |
|
| 1961 |
WAKE RG, BALDWIN RL. Analysis of casein fractions by zone electrophoresis in concentrated urea. Biochimica Et Biophysica Acta. 47: 225-39. PMID 13782592 DOI: 10.1016/0006-3002(61)90280-3 |
0.513 |
|
| 1960 |
Kirkwood JG, Baldwin RL, Dunlop PJ, Gosting LJ, Kegeles G. Flow equations and frames of reference for isothermal diffusion in liquids The Journal of Chemical Physics. 33: 1505-1513. DOI: 10.1063/1.1731433 |
0.654 |
|
| 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 DOI: 10.1016/0006-3002(58)90476-1 |
0.581 |
|
| 1958 |
Williams JW, Holde KEV, Baldwin RL, Fujita H. Part III. Fundamental Theory Of Sedimentation Processes In The Ultracentrifuge Chemical Reviews. 58: 784-806. DOI: 10.1021/Cr50022A007 |
0.494 |
|
| 1958 |
Williams JW, Holde KEV, Baldwin RL, Fujita H. Part II. Velocity Sedimentation Chemical Reviews. 58: 745-783. DOI: 10.1021/Cr50022A006 |
0.487 |
|
| 1958 |
Williams JW, Holde KEV, Baldwin RL, Fujita H. The Theory Of Sedimentation Analysis Chemical Reviews. 58: 715-744. DOI: 10.1021/Cr50022A005 |
0.491 |
|
| 1955 |
Baldwin RL, Gosting LJ, Williams JW, Alberty RA. Characterization and physical properties. Transport processes and the heterogeneity of proteins Discussions of the Faraday Society. 20: 13-24. DOI: 10.1039/Df9552000013 |
0.718 |
|
| 1955 |
Baldwin RL, Dunlop PJ, Gosting LJ. Interacting flows in liquid diffusion: Equations for evaluation of the diffusion coefficients from moments of the refractive index gradient curves Journal of the American Chemical Society. 77: 5235-5238. DOI: 10.1021/Ja01625A008 |
0.644 |
|
| 1952 |
Williams JW, Baldwin RL, Saunders WM, Squire PG. Boundary Spreading in Sedimentation Velocity Experiments. I. The Enzymatic Degradation of Serum Globulins Journal of the American Chemical Society. 74: 1542-1548. DOI: 10.1021/Ja01126A059 |
0.491 |
|
| 1951 |
BALDWIN RL, LAUGHTON PM, ALBERTY RA. Homogeneity and the electrophoretic behavior of some proteins. III A general method for the determination of mobility distributions. The Journal of Physical and Colloid Chemistry. 55: 111-25. PMID 14814637 DOI: 10.1021/J150484A013 |
0.497 |
|
| 1950 |
Baldwin RL, Williams JW. Boundary Spreading In Sedimentation Velocity Experiments Journal of the American Chemical Society. 72: 4325-4325. DOI: 10.1021/Ja01165A554 |
0.485 |
|
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