2001/03/19 by Ke Fan, K. Fan, J. Wang +3 · 1 citation
Biochemistry, Genetics and Molecular Biology · Materials Science · Physics and Astronomy · #Enzyme Structure and Function #Protein Structure and Dynamics #Theoretical and Computational Physics #cond-mat.soft #cond-mat.stat-mech #q-bio
paper · pdf · doi:10.1103/physreve.64.041907
published as Phys. Rev. E, 64 (2001) 041907 · 5 figures
arxiv created 2001/03/19 · openalex publication_date 2001/09/21 · arxiv updated 2009/11/30 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/28
A protein model with the pairwise interaction energies varying as the local environment changes, i.e., including some kind of collective effect between the contacts, is proposed. Lattice Monte Carlo simulations on the thermodynamical characteristics and free energy profile show a well-defined two-state behavior and cooperativity of folding for such a model. As a comparison, related simulations for the usual G&o model, where the interaction energies are independent of the local conformation, are also made. Our results indicate that the evolution of interactions during the folding process plays an important role in the two-state cooperativity in protein folding.