Packing interactions in the apomyglobin folding intermediate

被引：178

作者：

Kay, MS ^{[1
]}

Baldwin, RL ^{[1
]}

机构：

[1] STANFORD UNIV,MED CTR,DEPT BIOCHEM,STANFORD,CA 94305

来源：

NATURE STRUCTURAL BIOLOGY | 1996年 / 3卷 / 05期

关键词：

D O I：

10.1038/nsb0596-439

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 contribution of specific packing to the stability of the sperm whale apomyoglobin intermediate has been studied by urea denaturation monitored by circular dichroism and fluorescence. Mutations disrupting native packing sites within the subdomain formed by the A, G and H helices destabilize the intermediate, in contrast to the conclusion drawn from earlier studies of pH-induced unfolding. Based on these results, the intermediate is proposed to be stabilized by both partially formed native-like tertiary, and non-specific hydrophobic interactions forming a subdomain folding intermediate. The results help to explain how the intermediate acquires its structure and stability.

引用

页码：439 / 445

页数：7

共 38 条

[31] UNFOLDING FREE-ENERGY CHANGES DETERMINED BY THE LINEAR EXTRAPOLATION METHOD .1. UNFOLDING OF PHENYLMETHANESULFONYL ALPHA-CHYMOTRYPSIN USING DIFFERENT DENATURANTS [J].