Exploring Structure, Dynamics, and Topology of Nitroxide Spin-Labeled Proteins Using Continuous-Wave Electron Paramagnetic Resonance Spectroscopy

被引：60
|
作者：
Altenbach, Christian [1 ]
Lopez, Carlos J. [1 ]
Hideg, Kalman [2 ]
Hubbell, Wayne L. [1 ]
机构：
[1] Univ Calif Los Angeles, Jules Stein Eye Inst, Dept Chem & Biochem, Los Angeles, CA 90024 USA
[2] Univ Pecs, Inst Organ & Med Chem, Pecs, Hungary
来源：
ELECTRON PARAMAGNETIC RESONANCE INVESTIGATIONS OF BIOLOGICAL SYSTEMS BY USING SPIN LABELS, SPIN PROBES, AND INTRINSIC METAL IONS, PT B | 2015年 / 564卷
关键词：
LIGHT-DEPENDENT CHANGES; SIDE-CHAINS; T4; LYSOZYME; DISTANCE MEASUREMENTS; CONFORMATIONAL EXCHANGE; SATURATION RECOVERY; MEMBRANE-PROTEINS; PHYSIOLOGICAL TEMPERATURES; BACKBONE DYNAMICS; MOTION;
D O I：
10.1016/bs.mie.2015.08.006
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Structural and dynamical characterization of proteins is of central importance in understanding the mechanisms underlying their biological functions. Site-directed spin labeling (SDSL) combined with continuous-wave electron paramagnetic resonance (CW EPR) spectroscopy has shown the capability of providing this information with site-specific resolution under physiological conditions for proteins of any degree of complexity, including those associated with membranes. This chapter introduces methods commonly employed for SDSL and describes selected CW EPR-based methods that can be applied to (1) map secondary and tertiary protein structure, (2) determine membrane protein topology, (3) measure protein backbone flexibility, and (4) reveal the existence of conformational exchange at equilibrium.
引用
收藏
页码：59 / 100
页数：42
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