Collège Doctoral - Doktorandenkollegien

Statistical Physics of Complex Systems

Coventry - Leipzig - Lviv - Nancy

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Publication

Title Two-State Folding, Folding through Intermediates, and Metastability in a Minimalistic Hydrophobic-Polar Model for Proteins
Authors S. Schnabel, M. Bachmann, and W. Janke
Reference Phys. Rev. Lett. 98 (2007) 048103(1-4)
DOI10.1103/PhysRevLett.98.048103
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.


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