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Peng, Z Y; Wu, L C; Kim, P S (1995) Local structural preferences in the alpha-lactalbumin molten globule. Biochemistry 34:3248-52
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Wu, L C; Peng, Z Y; Kim, P S (1995) Bipartite structure of the alpha-lactalbumin molten globule. Nat Struct Biol 2:281-6
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Peng, Z Y; Wu, L C; Schulman, B A et al. (1995) Does the molten globule have a native-like tertiary fold? Philos Trans R Soc Lond B Biol Sci 348:43-7
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Yu, M H; Weissman, J S; Kim, P S (1995) Contribution of individual side-chains to the stability of BPTI examined by alanine-scanning mutagenesis. J Mol Biol 249:388-97
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Schulman, B A; Kim, P S (1994) Hydrogen exchange in BPTI variants that do not share a common disulfide bond. Protein Sci 3:2226-32
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Lumb, K J; Kim, P S (1994) Formation of a hydrophobic cluster in denatured bovine pancreatic trypsin inhibitor. J Mol Biol 236:412-20
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Staley, J P; Kim, P S (1994) Formation of a native-like subdomain in a partially folded intermediate of bovine pancreatic trypsin inhibitor. Protein Sci 3:1822-32
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Staley, J P; Kim, P S (1992) Complete folding of bovine pancreatic trypsin inhibitor with only a single disulfide bond. Proc Natl Acad Sci U S A 89:1519-23
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Weissman, J S; Kim, P S (1992) Kinetic role of nonnative species in the folding of bovine pancreatic trypsin inhibitor. Proc Natl Acad Sci U S A 89:9900-4
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Weissman, J S; Kim, P S (1992) The pro region of BPTI facilitates folding. Cell 71:841-51
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