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Science 20 September 1991:
Vol. 253. no. 5026, pp. 1386 - 1393
DOI: 10.1126/science.1716783
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Articles

Science, Vol 253, Issue 5026, 1386-1393
Copyright © 1991 by American Association for the Advancement of Science

articles

Reexamination of the folding of BPTI: predominance of native intermediates

JS Weissman and PS Kim

Howard Hughes Medical Institute, Whitehead Institute for Biomedical Research, Cambridge, MA 02142.

Bovine pancreatic trypsin inhibitor (BPTI) continues to be the only protein for which a detailed pathway of folding has been described. Previous studies led to the conclusion that nonnative states are well populated in the oxidative folding of BPTI. This conclusion has broadly influenced efforts to understand protein folding. The population of intermediates present during the folding of BPTI has been reexamined by modern separation techniques. It was found that all well-populated folding intermediates contain only native disulfide bonds. These data emphasize the importance of native protein structure for understanding protein folding.


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Salt-induced detour through compact regions of the protein folding landscape.
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An entropy criterion to detect minimally frustrated intermediates in native proteins.
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Endocrinopathies in the Family of Endoplasmic Reticulum (ER) Storage Diseases: Disorders of Protein Trafficking and the Role of ER Molecular Chaperones.
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Kinetic Intermediates Trapped by Native Interactions in RNA Folding.
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Science 279, 1943-1946
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Influenza hemagglutinin is spring-loaded by a metastable native conformation.
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Refolding Process of Ovalbumin from Urea-denatured State. EVIDENCE FOR THE INVOLVEMENT OF NONPRODUCTIVE SIDE CHAIN INTERACTIONS IN AN EARLY INTERMEDIATE.
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J. Biol. Chem. 272, 3973-3979
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A Two-Stage Mechanism for the Reductive Unfolding of Disulfide-containing Proteins.
J.-Y. Chang and J. Y. Chang (1997)
J. Biol. Chem. 272, 69-75
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Refolding and Oxidation of Recombinant Human Stem Cell Factor Produced in Escherichia coli.
M. D. Jones, L. O. Narhi, W.-C. Chang, and H. S. Lu (1996)
J. Biol. Chem. 271, 11301-11308
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Occurrence of Transient Multimeric Species during the Refolding of a Monomeric Protein.
F.édér. Pecorari, P. Minard, M. Desmadril, and J. M. Yon (1996)
J. Biol. Chem. 271, 5270-5276
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Structural and Functional Characteristics of Partially Disulfide-reduced Intermediates of Ovotransferrin N Lobe.
H. Yamashita, T. Nakatsuka, and M. Hirose (1995)
J. Biol. Chem. 270, 29806-29812
   Abstract »    Full Text »    PDF »
The Essential Function of Protein-disulfide Isomerase Is to Unscramble Non-native Disulfide Bonds.
M. C. A. Laboissière, S. L. Sturley, and R. T. Raines (1995)
J. Biol. Chem. 270, 28006-28009
   Abstract »    Full Text »    PDF »
The Properties of Scrambled Hirudins.
J.-Y. Chang and J. Y. Chang (1995)
J. Biol. Chem. 270, 25661-25666
   Abstract »    Full Text »    PDF »
The Disulfide Folding Pathway of Human Epidermal Growth Factor.
J.-Y. Chang, P. Schindler, U. Ramseier, and P.-H. Lai (1995)
J. Biol. Chem. 270, 9207-9216
   Abstract »    Full Text »    PDF »
Glutaredoxin Accelerates Glutathione-dependent Folding of Reduced Ribonuclease A Together with Protein Disulfide-isomerase.
J. Lundström-Ljung and A. Holmgren (1995)
J. Biol. Chem. 270, 7822-7828
   Abstract »    Full Text »    PDF »
DsbA-mediated Disulfide Bond Formation and Catalyzed Prolyl Isomerization in Oxidative Protein Folding.
C. Frech and F. X. Schmid (1995)
J. Biol. Chem. 270, 5367-5374
   Abstract »    Full Text »    PDF »
The disulfide folding pathway of BPTI.
T. Creighton (1992)
Science 256, 111-114
   PDF »
Response.
J. S. Weissman and P. S. Kim (1992)
Science 256, 112-114
   PDF »
Molecular self-assembly and nanochemistry: a chemical strategy for the synthesis of nanostructures.
G. Whitesides, J. Mathias, and C. Seto (1991)
Science 254, 1312-1319
   Abstract »    PDF »
A Major Kinetic Trap for the Oxidative Folding of Human Epidermal Growth Factor.
J.-Y. Chang, L. Li, and P.-H. Lai (2001)
J. Biol. Chem. 276, 4845-4852
   Abstract »    Full Text »    PDF »
Mutations in the N- and C-terminal Tails of Potato Carboxypeptidase Inhibitor Influence Its Oxidative Refolding Process at the Reshuffling Stage.
G. Venhudova, F. Canals, E. Querol, and F. X. Aviles (2001)
J. Biol. Chem. 276, 11683-11690
   Abstract »    Full Text »    PDF »


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Science. ISSN 0036-8075 (print), 1095-9203 (online)