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Simple models of polypeptides – conformational properties. A Monte Carlo study
Author(s) -
Sikorski Andrzej,
Romiszowski Piotr
Publication year - 2002
Publication title -
macromolecular symposia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.257
H-Index - 76
eISSN - 1521-3900
pISSN - 1022-1360
DOI - 10.1002/1521-3900(200205)181:1<327::aid-masy327>3.0.co;2-n
Subject(s) - monte carlo method , replica , chain (unit) , materials science , simple (philosophy) , statistical physics , lattice (music) , crystallography , chemical physics , chemistry , physics , mathematics , art , philosophy , statistics , epistemology , astronomy , acoustics , visual arts
A simple model of polypeptide chains was studied by means of Monte Carlo method. The chains were built on the (310) hybrid lattice and were represented by united atoms centered on alpha carbons. The residues interacted with the long‐range potential. The model chain consisted of two kinds of residues only: hydrophobic and hydrophilic forming a helical pattern ‐HHPPHPP‐. The classical sampling Metropolis and new Replica Exchange simulation methods were applied to study the model chains. It has been found that at low temperatures the model chain formed dense and partially ordered but not unique structures. The characteristics of the coil‐to‐globule transition was determined.