Structure of a kinetic protein folding intermediate by equilibrium amide exchange

被引：37

作者：

Hosszu, LLP

Craven, CJ

Parker, MJ

Lorch, M

Spencer, J

Clarke, AR

Waltho, JP

机构：

[1] UNIV SHEFFIELD,KREBS INST BIOMOLEC RES,DEPT MOL BIOL & BIOTECHNOL,SHEFFIELD S10 2UH,S YORKSHIRE,ENGLAND

[2] UNIV BRISTOL,SCH MED SCI,DEPT BIOCHEM,BRISTOL BS8 1TD,AVON,ENGLAND

来源：

NATURE STRUCTURAL BIOLOGY | 1997年 / 4卷 / 10期

关键词：

D O I：

10.1038/nsb1097-801

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：

A combination of equilibrium amide exchange and kinetic folding data show that the essential features of the complex topology of the N-terminal domain of a thermophilic phosphoglycerate kinase are established on a millisecond or faster timescale, before the rate-limiting step in the folding pathway commences.

引用

收藏

页码：801 / 804

页数：4

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