HYDROGEN-EXCHANGE RATES AND PROTEIN-FOLDING

被引：85

作者：

WOODWARD, CK

机构：

[1] Dept. of Biochemistry, University of Minnesota, St Paul, MN 55108

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 1994年 / 4卷 / 01期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/S0959-440X(94)90068-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：

Transient folding intermediates have been monitored in 11 proteins by pulsed hydrogen exchange methods. Standard hydrogen isotope exchange kinetics have also been measured for several molten globules. Taken together with folding kinetics detected by optical techniques, and with hydrogen exchange kinetics in native proteins, the results permit conclusions about time constants, structure and stability of folding intermediates, and about parallel versus serial folding pathways.

引用

页码：112 / 116

页数：5

共 34 条

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