Metastability of the folded states of globular proteins.
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.
Honeycutt
J D
JD
Department of Chemistry and Biochemistry, University of Maryland, College Park 20742.
Thirumalai
D
D
D004355:Drug Stability; D007700:Kinetics; D008958:Models, Molecular; D011487:Protein Conformation; D011506:Proteins; D013816:Thermodynamics
D011506:Proteins