Application of site-directed spin labelling for studying conformational changes in the catalytic cycle of G proteins activated by dimerization
Application of site-directed spin labelling for studying conformational changes in the catalytic cycle of G proteins activated by dimerization
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应用定点自旋标记研究二聚化激活的 G 蛋白催化循环中的构象变化
DOI：
10.1039/9781782629436-00157
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发表时间：
2016
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定点自旋标记（SDSL）结合电子顺磁共振（EPR）技术是研究蛋白质结构和构象动力学的有效方法。特别是，通过脉冲EPR方法的自旋标记对之间的长距离测量（高达B100 μ m）使得能够定量分析构象平衡动力学，并允许识别和表征蛋白质功能过程中的构象变化。本文综述了SDSL EPR对理解一组特定的GTP水解蛋白（由核苷酸依赖性二聚化（GADs）激活的G蛋白）的结构和动力学在其功能周期中的变化所做的贡献。
Site-directed spin labelling (SDSL) combined with electron paramagnetic resonance (EPR) spectroscopy is an efficient method to study the structure and the conformational dynamics of proteins. In particular, long range distance measurements (up to B100 Å) between pairs of spin labels by pulse EPR methods enable quantitative analysis of conformational equilibrium dynamics and allow identification and characterization of conformational changes in the course of a proteins function. This review summarizes contributions SDSL EPR made to understanding of how the structure and dynamics of a specific group of GTP-hydrolyzing proteins, G proteins activated by nucleotidedependent dimerization (GADs), change during their functional cycle.