Journal
PROTEIN SCIENCE
Volume 13, Issue 3, Pages 822-829Publisher
WILEY
DOI: 10.1110/ps.03403604
Keywords
protein folding kinetics; two-state folding; folding cooperativity; Phi-value analysis; effective contact order; loop-closure entropy; master equation
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We 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 C12, 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.
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