Monte carlo simulations of protein-like heteropolymers.
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.
Sikorski
A
A
Department of Chemistry, University of Warsaw, Poland. sikorski@chem.uw.edu.pl
Romiszowski
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P
D000465:Algorithms; D003198:Computer Simulation; D006358:Hot Temperature; D008958:Models, Molecular; D008962:Models, Theoretical; D009010:Monte Carlo Method; D011108:Polymers / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D013696:Temperature
D011108:Polymers; D011506:Proteins