title: Metastability of the folded states of globular proteins.
abstract: The possibility that several metastable minima exist in which the folded forms of a polypeptide chain have similar structural characteristics but different energies is suggested. The validity of this hypothesis is illustrated with the aid of simulation methods on a model protein that folds into a beta-barrel structure. Some implications of this hypothesis such as the existence of multiple pathways with intermediates for protein folding are discussed.
authors.affiliation: Department of Chemistry and Biochemistry, University of Maryland, College Park 20742.
authors.forename: J D
authors.initials: JD
authors.lastname: Honeycutt
authors.forename: D
authors.initials: D
authors.lastname: Thirumalai
mesh_terms: D004355:Drug Stability; D007700:Kinetics; D008958:Models, Molecular; D011487:Protein Conformation; D011506:Proteins; D013816:Thermodynamics
chemical_list: D011506:Proteins