title: Molten globules, entropy-driven conformational change and protein folding.
abstract: The exquisite side chain close-packing in the protein core and at binding interfaces has prompted a conviction that packing selectivity is the primary mechanism for molecular recognition in folding and/or binding reactions. Contrary to this view, molten globule proteins can adopt native topology and bind targets tightly and specifically in the absence of side chain close-packing. The molten globule is a highly dynamic form with native-like secondary structure and a loose protein core that admits solvent. The related (but still controversial) dry molten globule is an expanded form of the native protein with largely intact topology but a tighter protein core that excludes solvent. Neither form retains side chain close-packing, and therefore both structure and function must result from other factors, assuming that the reality of the dry molten globule is accepted. This simplifying realization calls for a re-evaluation of established models.
authors.affiliation: Department of Biochemistry, Stanford University Medical Center, Stanford, CA 94305-5307, United States. baldwinb@stanford.edu
authors.forename: Robert L
authors.initials: RL
authors.lastname: Baldwin
authors.forename: George D
authors.initials: GD
authors.lastname: Rose
mesh_terms: D008024:Ligands; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D008024:Ligands; D011506:Proteins