STRATEGIES FOR THE STUDY OF CYTOCHROME-C STRUCTURE AND FUNCTION BY SITE-DIRECTED MUTAGENESIS

被引：16

作者：

CAFFREY, MS

机构：

[1] Institut de Biologie Structurale, 38027 Grenoble Cedex, 41, avenue des Martyrs

来源：

BIOCHIMIE | 1994年 / 76卷 / 07期

关键词：

CYTOCHROME C(2); ELECTRON TRANSFER; PROTEIN STABILITY; REDOX POTENTIAL;

D O I：

10.1016/0300-9084(94)90139-2

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 class I cytochromes c have been extensively studied by biochemical and biophysical methods; however, many questions remain concerning the roles of specific amino acids in electron transfer and stability properties. The method of site-directed mutagenesis, which substitutes specific amino acid residues by genetic methods, is ideal for addressing these questions of cytochrome c structure and function. Practical considerations of mutational effects on protein processing and stability will be addressed. The criteria for the selection of mutation sites will be discussed. Examples of site-directed mutagenesis studies, which were designed to elucidate the factors controlling biological electron transfer, protein processing, and protein stability, are given.

引用

页码：622 / 630

页数：9

共 49 条

[1] TEMPERATURE-SENSITIVE MUTATIONS OF BACTERIOPHAGE-T4 LYSOZYME OCCUR AT SITES WITH LOW MOBILITY AND LOW SOLVENT ACCESSIBILITY IN THE FOLDED PROTEIN [J].