Conformational specificity of trigger factor for the folding intermediates of α-lactalbumin

被引：20

作者：

Huang, GC ^{[1
]}

Li, ZY ^{[1
]}

Zhou, JM ^{[1
]}

机构：

[1] Acad Sinica, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 2000年 / 1480卷 / 1-2期

关键词：

assisted protein folding; trigger factor; alpha-lactalbumin; conformational derivative;

D O I：

10.1016/S0167-4838(00)00094-7

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：

To understand the structural features of polypeptides recognized by trigger factor, a number of conformational derivatives of alpha LA were prepared and their effects on the trigger factor assisted refolding of GAPDH were investigated. It was found that the conformers of alpha LA that efficiently reduce the trigger factor assisted reactivation of guanidine-denatured GAPDH by competitively binding with trigger factor are those derivatives that have loose structure. This suggests that trigger factor binds mainly to intermediates formed early during folding of GAPDH. (C) 2000 Elsevier Science B.V. All rights reserved.

引用

页码：77 / 82

页数：6

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