Multiple intermediates and transition states during protein unfolding

被引：105

作者：

Zaidi, FN ^{[1
]}

Nath, U ^{[1
]}

Udgaonkar, JB ^{[1
]}

机构：

[1] INDIAN INST SCI,TIFR CTR,BANGALORE 560012,KARNATAKA,INDIA

来源：

NATURE STRUCTURAL BIOLOGY | 1997年 / 4卷 / 12期

关键词：

D O I：

10.1038/nsb1297-1016

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：

Rapid kinetic studies of the unfolding of the small protein barstar by urea have been used to demonstrate the presence of at least two unfolding intermediates on two competing unfolding pathways. One intermediate has native-like secondary structure but has a partially solvated hydrophobic core, while the other is devoid of considerable secondary structure but has an intact hydrophobic core. It is shown that the transition states on the two pathways are very dissimilar structurally, but very similar energetically.

引用

页码：1016 / 1024

页数：9

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