Kinetic studies of β-sheet protein folding

被引：55

作者：

Capaldi, AP ^{[1
]}

Radford, SE ^{[1
]}

机构：

[1] Univ Leeds, Sch Biochem & Mol Biol, Leeds LS2 9JT, W Yorkshire, England

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 1998年 / 8卷 / 01期

基金：

英国惠康基金;

关键词：

D O I：

10.1016/S0959-440X(98)80014-6

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：

New studies have shown that folding of beta-sheet proteins can occur with and without intermediates, with fast to slow refolding rates and late to very late transition states. These experiments demonstrate that, despite early speculation to the contrary, beta-sheet protein folding does not appear to be fundamentally different from that of helical and mixed alpha,beta proteins.

引用

页码：86 / 92

页数：7

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