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On foldable protein-like models; a statistical-mechanical study with Monte Carlo simulations

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  • Hao, Ming-Hong
  • Scheraga, Harold A.

Abstract

This is study of a class of lattice polymer models which have a singular lowest-energy conformation and undergo a phase transition from the statistically random state to the unique ground state. Such foldable lattice polymers can be considered as a crude model for protein molecules. The procedure for constructing a foldable polymer model, including selection of the monomer sequence and optimization of the force field, is described. A solvation term for individual monomers was added to the pairwise contact-based potential commonly used for the lattice polymer model. It is shown that the solvation interactions of individual residues make an important contribution to the folding of protein-like models. The statistical-mechanical characteristics of the models were analyzed with the help of Monte Carlo simulations. The model provides many insights to the protein-folding problem.

Suggested Citation

  • Hao, Ming-Hong & Scheraga, Harold A., 1997. "On foldable protein-like models; a statistical-mechanical study with Monte Carlo simulations," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 244(1), pages 124-146.
    • Handle: RePEc:eee:phsmap:v:244:y:1997:i:1:p:124-146
    DOI: 10.1016/S0378-4371(97)00222-7
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    References listed on IDEAS

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    1. Eun, Cheol S. & Kolodny, Richard & Scheraga, Carl, 1996. "Cross-border acquisitions and shareholder wealth: Tests of the synergy and internalization hypotheses," Journal of Banking & Finance, Elsevier, vol. 20(9), pages 1559-1582, November.
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    Cited by:

    1. Kozyrev, S.V. & Volovich, I.V., 2014. "Quinary lattice model of secondary structures of polymers," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 393(C), pages 86-95.

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