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Noninteracting local‐structure model of folding and unfolding transition in globular proteins. II. Application to two‐dimensional lattice proteins
Author(s) -
Abe Haruo,
GŌ Nobuhiro
Publication year - 1981
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1981.360200512
Subject(s) - globular protein , statistical physics , merge (version control) , lattice (music) , protein folding , chemistry , lattice model (finance) , monte carlo method , physics , lattice protein , chemical physics , crystallography , mathematics , computer science , biochemistry , statistics , acoustics , information retrieval
The noninteracting local‐structure model of the folding and unfolding transition in globular proteins, the formulation of which was given in the preceding paper, is applied to the analysis of the two‐dimensional lattice model of proteins. The lattice model of proteins is a theoretical tool designed to study the statistical‐mechanical aspect of the folding and unfolding transition. Its dynamics have been studied by a method of Monte Carlo simulation. The noninteracting local‐structure model reproduces the equilibrium properties of the lattice model obtained previously by computer simulation remarkably well, when the specificity of the long‐range interactions is strong. This observation indicates that the basic assumption of the noninteracting local‐structure model is equivalent to the assumption of strong specificity of intramolecular interactions. It is argued that by assuming this strong specificity, we can emphasize the correct main paths of folding and unfolding transition. The way local structures grow and/or merge along the most probable path of folding in the lattice model is discussed by the noninteracting local‐structure model.