Two-State Folding, Folding through Intermediates, and Metastability in a Minimalistic Hydrophobic-Polar Model for Proteins

摘要

Within the frame of an effective, coarse-grained hydrophobic-polar proteinmodel, we employ multicanonical Monte Carlo simulations to investigatefree-energy landscapes and folding channels of exemplified heteropolymersequences, which are permutations of each other. Despite the simplicity of themodel, the knowledge of the free-energy landscape in dependence of a suitablesystem order parameter enables us to reveal complex folding characteristicsknown from real bioproteins and synthetic peptides, such as two-state folding,folding through weakly stable intermediates, and glassy metastability.