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Thermodynamics of polypeptide model chains

Author

Listed:
  • Romiszowski, Piotr
  • Sikorski, Andrzej

Abstract

The model of a polypeptide chains was designed. The linear chain consisting of amino acid residues was approximated by an alpha carbon chain and embedded to a very flexible [310] lattice. The force field consisted of the long-range contact potential between residues and of the local helical potential. The chains were built of two types of amino acid residues, hydrophilic and hydrophobic forming a helical septets in the sequence. The Monte Carlo simulations of this model were carried out using the replica exchanges algorithm combined with the histogram method. The parameters describing the coil-to-globule transition were described and discussed. Thermodynamical properties of the polypeptide chains and of the folding transition were also determined.

Suggested Citation

  • Romiszowski, Piotr & Sikorski, Andrzej, 2004. "Thermodynamics of polypeptide model chains," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 336(1), pages 187-195.
  • Handle: RePEc:eee:phsmap:v:336:y:2004:i:1:p:187-195
    DOI: 10.1016/j.physa.2004.01.024
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