A combined EPR and MD simulation study of a nitroxyl spin label with restricted internal mobility sensitive to protein dynamics

Vasily S. Oganesyan, Fatima Chami, Gaye F. White, Andrew J. Thomson

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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.
Original languageEnglish
Pages (from-to)24–35
Number of pages12
JournalJournal of Magnetic Resonance
Early online date4 Nov 2016
Publication statusPublished - Jan 2017


  • EPR spectroscopy
  • spin labels
  • Molecular Dynamics simulations
  • MTSL
  • protein dynamics

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