Thermodynamical properties of simple models of protein-like heteropolymers.
The lattice approximation of a heteropolymer chain as a model of a single polypeptide was used in the computer simulation. The residues of a model polypeptide were represented by the chain of alpha-carbons located on a very flexible [310] lattice. The force field that mimic the intramolecular interactions contained the long-range contact potential between the residues and the local preferences in forming helical structures. The chain consisted of two types of residues that had different hydrophobicity. The simulations were performed by means of the Replica Exchange Monte Carlo method combined with the Histogram method. The series of simulations were carried out to investigate the influence of both components of the force field on the transition temperature and the characteristics of the coil-to-globule transition. The properties of low-temperature ordered structures were determined. The thermodynamical description of the model chain was also given. The phase transition was found to be sharp and cooperative for longer chains and strong helical potential. The collapsed globule contained the strongly hydrophobic residues inside the globule while the remaining residues were mainly located close to the globule surface.
Sikorski
Andrzej
A
Department of Chemistry, University of Warsaw, Pasteura 1, 02-093 Warsaw, Poland.
Romiszowski
Piotr
P
D001216:Asparagine / Q000737:chemistry; D001704:Biopolymers / Q000737:chemistry*; D008958:Models, Molecular; D009010:Monte Carlo Method; D010446:Peptide Fragments / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D013696:Temperature; D013816:Thermodynamics
D001704:Biopolymers; D010446:Peptide Fragments; D011506:Proteins; D001216:Asparagine