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| REEXAMINATION OF THE FOLDING OF BPTI - PREDOMINANCE OF NATIVE INTERMEDIATES |
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| Author(s): WEISSMAN JS, KIM PS |
| Source: SCIENCE Volume: 253 Issue: 5026 Pages: 1386-1393 Published: SEP 20 1991 |
| Times Cited: 418 References: 46 |
| 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. |
| Document Type: Article |
| Language: English |
| Reprint Address: WEISSMAN, JS (reprint author), WHITEHEAD INST BIOMED RES, HOWARD HUGHES MED INST, 9 CAMBRIDGE CTR, CAMBRIDGE, MA 02142 USA |
Addresses:
1. MIT, DEPT PHYS, CAMBRIDGE, MA 02139 USA
2. MIT, DEPT BIOL, CAMBRIDGE, MA 02139 USA |
| Publisher: AMER ASSOC ADVANCEMENT SCIENCE, 1200 NEW YORK AVE, NW, WASHINGTON, DC 20005 |
| Subject Category: Multidisciplinary Sciences |
| IDS Number: GF851 |
| ISSN: 0036-8075 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |