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Application of site-directed spin labelling for studying conformational changes in the catalytic cycle of G proteins activated by dimerization

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 ∼100 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 nucleotide-dependent dimerization (GADs), change during their functional cycle.

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01 Dec 2016
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