The burst phase in ribonuclease A folding and solvent dependence of the unfolded state

被引：139

作者：

Qi, PX ^{[1
]}

Sosnick, TR

Englander, SW

机构：

[1] Univ Penn, Sch Med, Johnson Res Fdn, Dept Biochem & Biophys, Philadelphia, PA 19104 USA

[2] Univ Chicago, Dept Biochem & Mol Biol, Chicago, IL 60637 USA

来源：

NATURE STRUCTURAL BIOLOGY | 1998年 / 5卷 / 10期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1038/2321

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：

Submillisecond hurst phase signals measured in kinetic protein folding experiments have been widely interpreted in terms of the fast formation of productive folding intermediates. Experimental comparisons with non-folding polypeptide chains show that, for ribonuclease A and cytochrome c, these signals in fact reflect a shift from one biased ensemble of the unfolded state to another as a function of change in denaturant concentration.

引用

页码：882 / 884

页数：3

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