Kinetic intermediates in the formation of the cytochrome c molten globule

被引:94
作者
Colon, W
Roder, H
机构
[1] FOX CHASE CANC CTR,INST CANC RES,PHILADELPHIA,PA 19111
[2] UNIV PENN,DEPT BIOCHEM & BIOPHYS,PHILADELPHIA,PA 19104
来源
NATURE STRUCTURAL BIOLOGY | 1996年 / 3卷 / 12期
关键词
D O I
10.1038/nsb1296-1019
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 relationship between molten globules and transient intermediates in protein folding has been explored by equilibrium and kinetic analysis of the compact acid-denatured A-state of cytochrome c. The chloride-induced formation of the A-state is a complex reaction with structural intermediates resembling those found under native refolding conditions, including a rapidly formed compact state and a subsequent intermediate with interacting N- and C-terminal helices. Together with mutational evidence for specific helix-helix packing interactions, this shows that the A-state is a stable analogue of a late folding intermediate. The L94A mutation blocks all folding steps after the initial collapse and its equilibrium state resembles early kinetic intermediates.
引用
收藏
页码:1019 / 1025
页数:7
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