Kinetic role of early intermediates in protein folding.
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.
Roder
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Institute for Cancer Research, Fox Chase Cancer Center, Philadelphia, PA 19111, USA. H_Roder@fccc.edu
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D005456:Fluorescent Dyes; D007700:Kinetics; D016297:Mutagenesis, Site-Directed; D017510:Protein Folding; D017433:Protein Structure, Secondary; D012997:Solvents
D005456:Fluorescent Dyes; D012997:Solvents