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Chevron rollovers of some proteins imply that their logarithmic folding ratesare nonlinear in native stability. This is predicted by lattice and continuumG\=o models to arise from diminished accessibilities of the ground state fromtransiently populated compact conformations under strongly native conditions.Despite these models' native-centric interactions, the slowdown is due partlyto kinetic trapping caused by some of the folding intermediates' nonnativetopologies. Notably, simple two-state folding kinetics of small single-domainproteins are not reproduced by common G\=o-like schemes.Comment: 10 pages, 4 Postscript figures (will appear on PRL

Origins of Chevron Rollovers in Non-Two-State Protein Folding Kinetics