Proline cis-trans isomerization and protein folding

被引：384

作者：

Wedemeyer, WJ ^{[1
]}

Welker, E ^{[1
]}

Scheraga, HA ^{[1
]}

机构：

[1] Cornell Univ, Baker Lab Chem & Chem Biol, Ithaca, NY 14853 USA

来源：

BIOCHEMISTRY | 2002年 / 41卷 / 50期

关键词：

D O I：

10.1021/bi020574b

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：

Proline cis-trans isomerization plays a key role in the rate-determining steps of protein folding. The energetic origin of this isomerization process is summarized, and the folding and unfolding of disulfide-intact bovine pancreatic ribonuclease A is used as an example to illustrate the kinetics and structural features of conformational changes from the heterogeneous unfolded state (consisting of cis and trans isomers of X-Pro peptide groups) to the native structure in which only one set of proline isomers is present.

引用

页码：14637 / 14644

页数：8

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