title: Solvent damping of internal processes in myoglobin studied by specific heat spectroscopy and flash photolysis.
abstract: We address the question of dynamic coupling between protein and solvent by comparing the enthalpy relaxation of the solvent (75% v/v glycerol-water) to internal ligand binding in myoglobin. When the solvent relaxation is slow compared to intramolecular events we observe decoupling of protein motions from the solvent. In the opposite limit there is a significant contribution of the solvent to internal friction. The solvent enhances the apparent activation energy of transitions in myoglobin. This result is discussed in terms of a generalized Kramer's law involving a dynamic friction coefficient.
authors.affiliation: Technische Universität München, Physik-Department E13, Garching, FRG.
authors.forename: M
authors.initials: M
authors.lastname: Settles
authors.forename: F
authors.initials: F
authors.lastname: Post
authors.forename: D
authors.initials: D
authors.lastname: Müller
authors.forename: A
authors.initials: A
authors.lastname: Schulte
authors.forename: W
authors.initials: W
authors.lastname: Doster
mesh_terms: D000818:Animals; D002151:Calorimetry; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D006736:Horses; D007700:Kinetics; D008956:Models, Chemical; D009211:Myoglobin / Q000737:chemistry*; D010782:Photolysis; D012997:Solvents; D013057:Spectrum Analysis; D013816:Thermodynamics
chemical_list: D009211:Myoglobin; D012997:Solvents