title: Kinetic role of early intermediates in protein folding.
abstract: The traditional view that partly folded intermediates are important for directing a protein toward the native state has been challenged by the notion that proteins can intrinsically fold rapidly in a single step if kinetic complications due to slow conformational events are avoided. Intermediates that accumulate within the first few milliseconds of folding are, however, a common observation even for small single-domain proteins. Recent spectroscopic studies, coupled with quantitative kinetic analysis, suggest that folding is facilitated by the rapid formation of compact intermediates with some native-like structural features.
authors.affiliation: Institute for Cancer Research, Fox Chase Cancer Center, Philadelphia, PA 19111, USA. H_Roder@fccc.edu
authors.forename: H
authors.initials: H
authors.lastname: Roder
authors.forename: W
authors.initials: W
authors.lastname: Colón
mesh_terms: D005456:Fluorescent Dyes; D007700:Kinetics; D016297:Mutagenesis, Site-Directed; D017510:Protein Folding; D017433:Protein Structure, Secondary; D012997:Solvents
chemical_list: D005456:Fluorescent Dyes; D012997:Solvents