title: The water R1(ω) NMRD profiles of a hydrated protein from molecular dynamics simulation.
abstract: The hydration of a protein, Peroxiredoxin 5, is obtained from a molecular dynamics simulation and compared with the picture of hydration which is obtained by analysing the water proton R1 NMRD profiles using a generally accepted relaxation model [K. Venu, V. P. Denisov and B. Halle, J. Am. Chem. Soc., 1997, 119, 3122]. The discrepancy between the hydration pictures derived from the water R1(ω0)-NMRD profiles and MD is relevant in a discussion of the factors behind the stretched NMRD profile, the distribution of orientational order parameters and residence times of buried water used in the NMRD model.
authors.affiliation: Department of Chemistry, Umeå University, Umeå, Sweden.
authors.forename: Yang
authors.initials: Y
authors.lastname: Huang
authors.forename: Kwangho
authors.initials: K
authors.lastname: Nam
authors.forename: Per-Olof
authors.initials: PO
authors.lastname: Westlund
mesh_terms: D056004:Molecular Dynamics Simulation; D054464:Peroxiredoxins / Q000737:chemistry* / Q000378:metabolism; D017434:Protein Structure, Tertiary; D011522:Protons; D014867:Water / Q000737:chemistry*
chemical_list: D011522:Protons; D014867:Water; D054464:Peroxiredoxins