Abstract
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 A) 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.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
