A Monte Carlo study of properties of protein-like heteropolymers

Piotr Romiszowski and Andrzej Sikorski

Physica A: Statistical Mechanics and its Applications, 1999, vol. 273, issue 1, 190-197

Abstract: The structure of a polypeptide model by means of the Monte Carlo method has been studied. The model chains consisting of two kinds of residues (hydrophobic and hydrophilic) were confined on the (310) hybrid lattice. The residues interacted with the long-range contact potential. The short-range potential was also used by introducing the preferences of conformations corresponding to the helical structure. Simulations of the coil-to-globule collapse have been done by an annealing process starting from high-temperature structures and then gradual cooling of the system. It has been found that in a case of a helical pattern –HHPPHPP– the collapsed chains consisted of longer helical fragments. The results show the influence of the potentials used in a model on final static and dynamic properties of molecules.

Keywords: Protein folding; Protein model (search for similar items in EconPapers)
Date: 1999
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Persistent link: https://EconPapers.repec.org/RePEc:eee:phsmap:v:273:y:1999:i:1:p:190-197

DOI: 10.1016/S0378-4371(99)00354-4

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