Fractal protein structure revisited: Topological, kinetic and thermodynamic relationships

被引：17

作者：

Tejera, E. ^{[1
]}

Machado, A. ^{[1
]}

Rebelo, I. ^{[1
]}

Nieto-Villar, J. ^{[2
,3
]}

机构：

[1] Univ Porto, Fac Farm, Dept Bioquim, IBMC, Oporto, Portugal

[2] Univ La Habana, Fac Quim, Dept Quim Fis, Havana, Cuba

[3] Univ La Habana, Catedra Sistemas Complejos H Poincare, Havana, Cuba

来源：

PHYSICA A-STATISTICAL MECHANICS AND ITS APPLICATIONS | 2009年 / 388卷 / 21期

关键词：

Fractal dimension; Protein length; Thermodynamic; Folding rate; Spectral dimension; Contact map; FOLDING RATE; SECONDARY STRUCTURE; CONTACT ORDER; CHAIN-LENGTH; RATES; DETERMINANTS; SEQUENCES; STABILITY; MODEL; SIZE;

D O I：

10.1016/j.physa.2009.07.015

中图分类号：

O4 [物理学];

学科分类号：

0702 ;

摘要：

The present work explored the definitions and calculations of fractal dimensions in protein structures and the corresponding relationships with the protein class, secondary structure contents, fold type as well as kinetic and thermodynamic parameters like the folding and unfolding rate, the folding-unfolding free energy and others. The results showed a positive correlation of some fractal exponents with the kinetic and thermodynamic variables even considering the effect of the protein length. On the other hand the influences of secondary structures types, especially the turn conformation are significant as well as the fractal exponent profiles according to class and fold types. (C) 2009 Elsevier B.V. All rights reserved.

引用

页码：4600 / 4608

页数：9

共 27 条

[1] The Protein Data Bank [J].