A Monte Carlo study of properties of protein-like heteropolymers

被引：15

作者：

Romiszowski, P ^{[1
]}

Sikorski, A ^{[1
]}

机构：

[1] Univ Warsaw, Dept Chem, PL-02093 Warsaw, Poland

来源：

PHYSICA A | 1999年 / 273卷 / 1-2期

关键词：

protein folding; protein model;

D O I：

10.1016/S0378-4371(99)00354-4

中图分类号：

O4 [物理学];

学科分类号：

0702 ;

摘要：

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 (3 1 0) 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. (C) 1999 Elsevier Science B.V. All rights reserved.

引用

页码：190 / 197

页数：8

共 14 条

[1] PRINCIPLES THAT GOVERN FOLDING OF PROTEIN CHAINS [J].