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Updated: Mar 12, 2026
Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion Channels
Published on: July 4, 2016
A combined EPR and MD simulation study of a nitroxyl spin label with restricted internal mobility sensitive to
Vasily S Oganesyan1, Fatima Chami1, Gaye F White1
1School of Chemistry, University of East Anglia, Norwich NR4 7TJ, United Kingdom.
Abstract:
EPR studies combined with fully atomistic Molecular Dynamics (MD) simulations and an MD-EPR simulation method provide evidence for intrinsic low rotameric mobility of a nitroxyl spin label, Rn, compared to the more widely employed label MTSL (R1). Both experimental and modelling results using two structurally different sites of attachment to Myoglobin show that the EPR spectra of Rn are more sensitive to the local protein environment than that of MTSL. This study reveals the potential of using the Rn spin label as a reporter of protein motions.
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