The use of the Rx spin label in orientation measurement on proteins, by EPR

M A Stevens; Johannes Erik McKay; J L S Robinson; Hassane El Mkami; Graham Murray Smith; D G Norman

doi:10.1039/c5cp04753f

The use of the Rx spin label in orientation measurement on proteins, by EPR

M A Stevens, Johannes Erik McKay, J L S Robinson, Hassane El Mkami, Graham Murray Smith, D G Norman

School of Physics and Astronomy

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Abstract

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.

Original language	English
Pages (from-to)	5799-5806
Journal	Physical Chemistry Chemical Physics
Volume	18
Issue number	8
Early online date	25 Sept 2015
DOIs	https://doi.org/10.1039/c5cp04753f
Publication status	Published - 28 Feb 2016

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10.1039/c5cp04753fLicence: CC BY-NC

McKay_2016_PCCP_RxSpin_CCBYNC-FinalPublishedVersion
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/).
Final published version, 2.39 MBLicence: CC BY-NC

Cite this

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title = "The use of the Rx spin label in orientation measurement on proteins, by EPR",

abstract = "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.",

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note = "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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AU - Smith, Graham Murray

AU - Norman, D G

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The use of the Rx spin label in orientation measurement on proteins, by EPR

Abstract

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State of the art pulse EPR instrumentati: State of the art pulse EPR instrumentation for long range distance measurements in biomacromolecules

EP/F0390034/1 The HIPER Project: Bringing the NMR Paradigm to ESR - The HIPER Project

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The use of the Rx spin label in orientation measurement on proteins, by EPR

Abstract

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Projects

State of the art pulse EPR instrumentati: State of the art pulse EPR instrumentation for long range distance measurements in biomacromolecules

EP/F0390034/1 The HIPER Project: Bringing the NMR Paradigm to ESR - The HIPER Project

Cite this