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

Abstract

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

10 pages, 1 figure

References in corpus (2)

• Substrate Specificity of Peptide Adsorption: A Model Study
• Substrate Adhesion of a Nongrafted Flexible Polymer in a Cavity

Cited by in corpus (6)

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• Conformational Mechanics of Polymer Adsorption Transitions at Attractive Substrates
• Thickness-dependent secondary structure formation of tubelike polymers
• Identification of Characteristic Protein Folding Channels in a Coarse-Grained Hydrophobic-Polar Peptide Model
• Thermodynamics and Kinetics of a Go Proteinlike Heteropolymer Model with Two-State Folding Characteristics
• Monte Carlo simulations of proteins in cages: influence of confinement on the stability of intermediate states