title: Diffusion-collision model for the folding kinetics of myoglobin.
abstract: The diffusion-collision model has been used to analyze the folding kinetics of myoglobin. The microdomains, which are the basic units that coalesce during the folding, are identified with the helices and the stabilizing contacts between helices are determined from the native structure. Both association and dissociation reactions are included and a range of stabilization parameters is investigated to determine the variation in overall rate and the relative contributions made by different intermediates during the folding process. In a comparison of folding to the native state and to the midpoint of the folding transition (i.e., 50% native protein at the completion of the reaction) significant differences in the contributing intermediates are found.
authors.affiliation: Department of Physics, Tufts University, Medford, Massachusetts 02155.
authors.forename: D
authors.initials: D
authors.lastname: Bashford
authors.forename: F E
authors.initials: FE
authors.lastname: Cohen
authors.forename: M
authors.initials: M
authors.lastname: Karplus
authors.forename: I D
authors.initials: ID
authors.lastname: Kuntz
authors.forename: D L
authors.initials: DL
authors.lastname: Weaver
mesh_terms: D004058:Diffusion; D007700:Kinetics; D008956:Models, Chemical; D009211:Myoglobin; D011487:Protein Conformation
chemical_list: D009211:Myoglobin