Use of EPR power saturation toanalyze the membrane-docking geometries of peripheral proteins: A applications to C2 domains

被引:52
作者
Malmberg, NJ [1 ]
Falke, JJ
机构
[1] Univ Colorado, Mol Biophys Program, Boulder, CO 80309 USA
[2] Univ Colorado, Dept Biochem & Chem, Boulder, CO 80309 USA
来源
ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE | 2005年 / 34卷
关键词
electron paramagnetic resonance; electron spin resonance; membrane proteins; site-directed spin labeling;
D O I
10.1146/annurev.biophys.34.040204.144534
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
Despite the central importance of peripheral membrane proteins to cellular signaling and metabolic pathways, the structures of protein-membrane interfaces remain largely inaccessible to high-resolution structural methods. In recent years a number of laboratories have contributed to the development of an electron paramagnetic resonance (EPR) power saturation approach that utilizes site-directed spin labeling to determine the key geometric parameters of membrane-docked proteins, including their penetration depths and angular orientations relative to the membrane surface. Representative applications to Ca(2+)-activated, membrane-docking C2 domains are described.
引用
收藏
页码:71 / 90
页数:24
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