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- W2088397672 endingPage "28" @default.
- W2088397672 startingPage "15" @default.
- W2088397672 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." @default.
- W2088397672 created "2016-06-24" @default.
- W2088397672 creator A5006585307 @default.
- W2088397672 creator A5036860380 @default.
- W2088397672 date "1997-02-01" @default.
- W2088397672 modified "2023-10-16" @default.
- W2088397672 title "Kinetic role of early intermediates in protein folding" @default.
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