The use of the Rx spin label in orientation measurement on proteins, by EPR
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The bipedal spin label Rx is more restricted in its conformation and dynamics than its monopodal counterpart R1. To systematically investigate the utility of the Rx label, we have attempted to comprehensively survey the attachment of Rx to protein secondary structures. We have examined the formation, structure and dynamics of the spin label in relation to the underlying protein in order to determine feasibility and optimum conditions for distance and orientation measurement by pulsed EPR. The labeled proteins have been studied using molecular dynamics, CW EPR, pulsed EPR distance measurement at X-band and orientation measurement at W-band. The utility of different modes and positions of attachment have been compared and contrasted.
Stevens , M A , McKay , J E , Robinson , J L S , El Mkami , H , Smith , G M & Norman , D G 2016 , ' The use of the Rx spin label in orientation measurement on proteins, by EPR ' Physical Chemistry Chemical Physics , vol 18 , no. 8 , pp. 5799-5806 . DOI: 10.1039/c5cp04753f
Physical Chemistry Chemical Physics
Copyright 2015 the Authors. This article is licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported Licence (http://creativecommons.org/licenses/by-nc/3.0/).
M.A.S. & J.E.M. would like to acknowledge funding from the EPSRC as part of the iMR-CDT. The Authors would like to acknowledge funding from The MRC UK, Grant G1100021, EPSRC Basic Technology EP/F039034/1, and from the Wellcome Trust 099149/Z/12/Z.
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