title: A combined EPR and MD simulation study of a nitroxyl spin label with restricted internal mobility sensitive to protein dynamics.
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.
authors.affiliation: School of Chemistry, University of East Anglia, Norwich NR4 7TJ, United Kingdom. Electronic address: v.oganesyan@uea.ac.uk.
authors.forename: Vasily S
authors.initials: VS
authors.lastname: Oganesyan
authors.affiliation: School of Chemistry, University of East Anglia, Norwich NR4 7TJ, United Kingdom.
authors.forename: Fatima
authors.initials: F
authors.lastname: Chami
authors.affiliation: School of Chemistry, University of East Anglia, Norwich NR4 7TJ, United Kingdom.
authors.forename: Gaye F
authors.initials: GF
authors.lastname: White
authors.affiliation: School of Chemistry, University of East Anglia, Norwich NR4 7TJ, United Kingdom.
authors.forename: Andrew J
authors.initials: AJ
authors.lastname: Thomson
mesh_terms: D003198:Computer Simulation; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods*; D006801:Humans; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D009211:Myoglobin / Q000737:chemistry; D009589:Nitrogen Oxides / Q000737:chemistry*; D011487:Protein Conformation; D013113:Spin Labels
chemical_list: D009211:Myoglobin; D009589:Nitrogen Oxides; D013113:Spin Labels; C039900:nitroxyl
keywords: EPR spectroscopy; MTSL; Molecular dynamics simulations; Protein dynamics; Spin labels