Cooperativity in two-state protein folding kinetics

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dc.creatorWeikl, Thomas R.
dc.creatorPalassini, Matteo
dc.creatorDill, Ken A.
dc.date2003-11-06
dc.date.accessioned2026-07-07T05:57:57Z
dc.date.available2026-07-07T05:57:57Z
dc.descriptionWe present a solvable model that predicts the folding kinetics of two-state proteins from their native structures. The model is based on conditional chain entropies. It assumes that folding processes are dominated by small-loop closure events that can be inferred from native structures. For CI2, the src SH3 domain, TNfn3, and protein L, the model reproduces two-state kinetics, and it predicts well the average Phi-values for secondary structures. The barrier to folding is the formation of predominantly local structures such as helices and hairpins, which are needed to bring nonlocal pairs of amino acids into contact.
dc.description9 pages, 6 figures, 1 table
dc.identifierhttps://arxiv.org/abs/q-bio/0311004
dc.identifierhttp://arxiv.org/abs/q-bio/0311004
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/88184
dc.subjectBiomolecules
dc.subjectStatistical Mechanics
dc.titleCooperativity in two-state protein folding kinetics
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