Abstract
Abstract
Intrinsically disordered proteins (IDPs) form a unique protein category characterized by the absence of a well-defined structure and by remarkable conformational flexibility. Electron Paramagnetic Resonance (EPR) spectroscopy combined with site-directed spin labeling (SDSL) is amongst the most suitable methods to unravel their structure and dynamics. This review summarizes the tremendous methodological developments in the area of SDSL EPR and its applications in protein research. Recent results on the intrinsically disordered Parkinson’s disease protein α-synuclein illustrate that the method has gained increasing attention in IDP research. SDSL EPR has now reached a level where broad application in this rapidly advancing field is feasible.
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Acknowledgements
I am indebted to C. Jao, J. Freed, G. Jeschke, and R. Langen for permission to reproduce figures. I wish to thank Dr. Martina Huber and Prof. Dr. Vinod Subramaniam for a longstanding cooperation, Marco Wassmer, Martin Spitzbarth, and Christian Hintze for designing figures, and Gunnar Jeschke and the EPR people in Konstanz for fruitful discussions.
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© 2011 Springer-Verlag Berlin Heidelberg
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Drescher, M. (2011). EPR in Protein Science. In: Drescher, M., Jeschke, G. (eds) EPR Spectroscopy. Topics in Current Chemistry, vol 321. Springer, Berlin, Heidelberg. https://doi.org/10.1007/128_2011_235
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DOI: https://doi.org/10.1007/128_2011_235
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