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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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