Hydrophobic models of protein folding and the thermodynamics of chain-boundary interactions

被引：3

作者：

Erzan, A ^{[1
]}

Tüzel, E

机构：

[1] Istanbul Tech Univ, Dept Phys, Fac Sci & Letters, TR-80626 Istanbul, Turkey

[2] Feza Gursey Inst, TR-81220 Istanbul, Turkey

[3] Univ Minnesota, Sch Phys & Astron, Minneapolis, MN 55455 USA

来源：

BRAZILIAN JOURNAL OF PHYSICS | 2003年 / 33卷 / 03期

关键词：

D O I：

10.1590/S0103-97332003000300018

中图分类号：

O4 [物理学];

学科分类号：

0702 ;

摘要：

We review some results concerning the energetic and dynamical consequences of taking a generic hydrophobic model of a random polypeptide chain, where the effective hydrophobic interactions are represented by Hookcan springs. Then we present a set of calculations on a microscopic model of hydrophobic interactions, investigating the behaviour of a hydrophobic chain in the vicinity of a hydrophobic boundary. We conclude with some speculations as to the thermodynamics of pre-biotic functions proteins may have discharged very early on in the evolutionary past.

引用

页码：573 / 588

页数：16

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