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Reexamination of the Folding of BPTI: Predominance of Native Intermediates

Weissman, Jonathan S., Kim, Peter S.·1991·Science

Abstract

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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Metadata

Authors
Weissman, J. S., & Kim, P. S.
Venue
Science
Published
1991-09-20
Volume
253
Issue
5026
Pages
1386-1393
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2073084525
Cited by
512
References
0
FWCI
15.09
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Reexamination of the Folding of BPTI: Predominance of Native Intermediates. https://app.cochat.ai/papers/10.1126/science.1716783
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Weissman, J. S., & Kim, P. S. (1991). Reexamination of the Folding of BPTI: Predominance of Native Intermediates. Science. https://doi.org/10.1126/science.1716783

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.