Preorganized secondary structure as an important determinant of fast protein folding

被引：205

作者：

Myers, JK ^{[1
]}

Oas, TG ^{[1
]}

机构：

[1] Duke Univ, Med Ctr, Dept Biochem, Durham, NC 27710 USA

来源：

NATURE STRUCTURAL BIOLOGY | 2001年 / 8卷 / 06期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1038/88626

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：

The folding and unfolding kinetics of the B-domain of staphylococcal protein A, a small three-helix bundle protein, were probed by NMR. The lineshape of a single histidine resonance was fit as a function of denaturant to give folding and unfolding rate constants. The B-domain folds extremely rapidly in a two-state manner, with a folding rate constant of 120,000 s(-1), making it one of the fastest-folding proteins known. Diffusion-collision theory predicts folding and unfolding rate constants that are in good agreement with the experimental values. The apparent rate constant as a function of denaturant ('chevron plot') is predicted within an order of magnitude. Our results are consistent with a model whereby fast-folding proteins utilize a diffusion-collision mechanism, with the preorganization of one or more elements of secondary structure in the unfolded protein.

引用

页码：552 / 558

页数：7

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