NATIVE AND NONNATIVE INTERMEDIATES IN THE BPTI FOLDING PATHWAY

被引：119

作者：

GOLDENBERG, DP

机构：

[1] Department of Biology, University of Utah, Salt Lake City

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 1992年 / 17卷 / 07期

关键词：

D O I：

10.1016/0968-0004(92)90405-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Recent studies of the disulfide-bonded intermediates in the refolding of bovine pancreatic trypsin inhibitor (BPTI) indicate that the most stable intermediates can take on much or all of the structure of the fully folded protein. Native-like structure in the intermediates probably causes steric inhibition of direct sequential formation of the three disulfides found in the native protein, thus accounting for the role of intramolecular rearrangements in the folding mechanism of this small protein.

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页码：257 / 261

页数：5

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