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

Abstract

Chevron rollovers of some proteins imply that their logarithmic folding rates are nonlinear in native stability. This is predicted by lattice and continuum Gō models to arise from diminished accessibilities of the ground state from transiently populated compact conformations under strongly native conditions. Despite these models' native-centric interactions, the slowdown is due partly to kinetic trapping caused by some of the folding intermediates' nonnative topologies. Notably, simple two-state folding kinetics of small single-domain proteins are not reproduced by common Gō-like schemes.

10 pages, 4 Postscript figures (will appear on PRL)

References in corpus (1)

• Protein folding mediated by solvation: water expelling and formation of the hydrophobic core occurs after the structure collapse

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