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
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
相关论文
共 21 条
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