Site-directed spin labeling of proteins for distance measurements in vitro and in cells

被引：74
|
作者：
Roser, P. [1 ,2 ]
Schmidt, M. J. [1 ,2 ]
Drescher, M. [1 ,2 ]
Summerer, D. [3 ]
机构：
[1] Univ Konstanz, Dept Chem, Zukunftskolleg, Univ Str 10, D-78457 Constance, Germany
[2] Univ Konstanz, Konstanz Res Sch Chem Biol, Univ Str 10, D-78457 Constance, Germany
[3] Tech Univ Dortmund, Dept Chem & Chem Biol, Otto Hahn Str 6, D-44227 Dortmund, Germany
来源：
ORGANIC & BIOMOLECULAR CHEMISTRY | 2016年 / 14卷 / 24期
关键词：
ELECTRON-ELECTRON RESONANCE; ESCHERICHIA-COLI-CELLS; UNNATURAL AMINO-ACID; EPR SPECTROSCOPY; SIDE-CHAINS; PULSED EPR; RELAXATION-ENHANCEMENT; CONFORMATIONAL-CHANGES; MEMBRANE TRANSPORTER; TRITYL RADICALS;
D O I：
10.1039/c6ob00473c
中图分类号：
O62 [有机化学];
学科分类号：
070303 ; 081704 ;
摘要：
Site-directed spin labeling (SDSL) in combination with electron paramagnetic resonance (EPR) spectroscopy allows studying the structure, dynamics, and interactions of proteins via distance measurements in the nanometer range. We here give an overview of available spin labels, the strategies for their introduction into proteins, and the associated potentials for protein structural studies in vitro and in the context of living cells.
引用
收藏
页码：5468 / 5476
页数：9
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