Identifying conformational changes with site-directed spin labeling

被引：720
作者：
Hubbell, WL [1 ]
Cafiso, DS
Altenbach, C
机构：
[1] Univ Calif Los Angeles, Jules Stein Eye Inst, Los Angeles, CA 90095 USA
[2] Univ Calif Los Angeles, Dept Chem & Biochem, Los Angeles, CA 90095 USA
[3] Univ Virginia, Dept Chem, Charlottesville, VA 22901 USA
来源：
NATURE STRUCTURAL BIOLOGY | 2000年 / 7卷 / 09期
关键词：
D O I：
10.1038/78956
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：
Site-direct spin labeling combined with electron paramagnetic resonance (EPR) spectroscopy is a powerful tool for detecting structural changes in proteins. This review provides examples that illustrate strategies for interpreting the data in terms of specific rearrangements in secondary and tertiary structure. The changes in the mobility and solvent accessibility of the spin label side chains, and in the distances between spin labels, report (i) rigid body motions of alpha-helices and beta-strands (ii) relative movements of domains and (iii) changes in secondary structure. Such events can be monitored in the millisecond timescale, making it possible to follow structural changes during function. There is no upper limit to the size of proteins that can be investigated, and only 50-100 picomoles of protein are required. These features make site-directed spin labeling an attractive approach for the study of structure and dynamics in a wide range of systems.
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收藏
页码：735 / 739
页数：5
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