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• W2079547549 abstract "We have studied folding mechanisms of three small globular proteins: crambin (CRN), chymotrypsin inhibitor 2 (CI2) and the fyn Src Homology 3 domain (SH3) which are modelled by a Go-like Hamiltonian with the Lennard-Jones interactions. It is shown that folding is dominated by a well-defined sequencing of events as determined by establishment of particular contacts. The order of events depends primarily on the geometry of the native state. Variations in temperature, coupling strengths and viscosity affect the sequencing scenarios to a rather small extent. The sequencing is strongly correlated with the distance of the contacting aminoacids along the sequence. Thus $alpha$-helices get established first. Crambin is found to behave like a single-route folder, whereas in CI2 and SH3 the folding trajectories are more diversified. The folding scenarios for CI2 and SH3 are consistent with experimental studies of their transition states." @default.
• W2079547549 created "2016-06-24" @default.
• W2079547549 creator A5040259634 @default.
• W2079547549 creator A5063643408 @default.
• W2079547549 date "2000-11-08" @default.
• W2079547549 modified "2023-09-27" @default.
• W2079547549 title "Sequencing of folding events in Go-type proteins" @default.
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• W2079547549 doi "https://doi.org/10.1063/1.1314868" @default.
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