Monte carlo simulations of protein-like heteropolymers. | Zendy

Andrzej Sikorski | Zendy; Piotr Romiszowski | Zendy

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Monte carlo simulations of protein-like heteropolymers.

Author(s) -

Andrzej Sikorski,

Piotr Romiszowski

Publication year - 2001

Publication title -

acta biochimica polonica

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.452

H-Index - 78

eISSN - 1734-154X

pISSN - 0001-527X

DOI - 10.18388/abp.2001_5113

Subject(s) - monte carlo method , chain (unit) , single chain , helicity , chemical physics , chemistry , lattice (music) , molecular dynamics , polypeptide chain , annealing (glass) , crystallography , materials science , statistical physics , physics , computational chemistry , thermodynamics , mathematics , organic chemistry , statistics , particle physics , astronomy , acoustics , antibody , immunology , biology , enzyme

Properties of a simple model of polypeptide chains were studied by the means of the Monte Carlo method. The chains were built on the (310) hybrid lattice. The residues interacted with long-range potential. There were two kinds of residues: hydrophobic and hydrophilic forming a typical helical pattern -HHPPHPP-. Short range potential was used to prefer helical conformations of the chain. It was found that at low temperatures the model chain formes dense and partially ordered structures (non-unique). The presence of the local potential led to an increase of helicity. The effect of the interplay between the two potentials was studied. After the collapse of the chain further annealing caused rearrangement of helical structures. Dynamic properties of the chain at low temperature depended strongly on the local chain ordering.

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