Role of cofactors in protein folding

被引：150

作者：

Wittung-Stafshede, P ^{[1
]}

机构：

[1] Tulane Univ, Dept Chem, New Orleans, LA 70118 USA

来源：

ACCOUNTS OF CHEMICAL RESEARCH | 2002年 / 35卷 / 04期

关键词：

D O I：

10.1021/ar010106e

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Although cofactors are essential components of many proteins to attain biological activity, the role of cofactors in protein folding is not well understood. Biophysical characterization of four types of cofactor-binding proteins (with copper, flavin moiety, iron-sulfur cluster, and heme cofactors, respectively) provides the following insights. (1) The presence of the cofactor often stabilizes the native protein. (2) The cofactor has the ability to interact specifically with the unfolded polypeptide. (3) The presence of the cofactor is sometimes essential for the polypeptide to fold. (4) Coordination of the cofactor prior to polypeptide folding can dramatically accelerate formation of the functional protein.

引用

页码：201 / 208

页数：8

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