title: Onsets of anharmonicity in protein dynamics.
abstract: Two onsets of anharmonicity are observed in the dynamics of the protein lysozyme. One at T approximately 100 K appears in all samples regardless of hydration level and is consistent with methyl group rotation. The second, the well-known dynamical transition at T approximately 200-230 K, is only observed at a hydration level h greater than approximately 0.2 and is ascribed to the activation of an additional relaxation process. Its variation with hydration correlates well with variations of catalytic activity suggesting that the relaxation process is directly related to the activation of modes required for protein function.
authors.affiliation: Department of Polymer Science, The University of Akron, Akron, OH 44325-3909, USA.
authors.forename: J H
authors.initials: JH
authors.lastname: Roh
authors.forename: V N
authors.initials: VN
authors.lastname: Novikov
authors.forename: R B
authors.initials: RB
authors.lastname: Gregory
authors.forename: J E
authors.initials: JE
authors.lastname: Curtis
authors.forename: Z
authors.initials: Z
authors.lastname: Chowdhuri
authors.forename: A P
authors.initials: AP
authors.lastname: Sokolov
mesh_terms: D003080:Cold Temperature; D004527:Egg Proteins / Q000737:chemistry*; D008956:Models, Chemical; D009113:Muramidase / Q000737:chemistry*; D013816:Thermodynamics; D014867:Water / Q000737:chemistry
chemical_list: D004527:Egg Proteins; D014867:Water; D009113:Muramidase