Theoretical analysis on thermal stability of a protein focused on the water entropy

被引：39

作者：

Amano, Ken-ichi ^{[1
]}

Yoshidome, Takashi ^{[1
]}

Harano, Yuichi ^{[2
]}

Oda, Koji ^{[3
]}

Kinoshita, Masahiro ^{[1
]}

机构：

[1] Kyoto Univ, Inst Adv Energy, Kyoto 6110011, Japan

[2] Osaka Univ, Inst Prot Res, Suita, Osaka 5650871, Japan

[3] Taisho Pharmaceut Co Ltd, Kita Ku, Saitama 3319530, Japan

来源：

CHEMICAL PHYSICS LETTERS | 2009年 / 474卷 / 1-3期

关键词：

ELECTROLYTE-SOLUTIONS; HIGH ASPHERICITY; SMALL SPHERES; IRON-BINDING; BIG BODIES; APPROXIMATION; DYNAMICS; BIOLOGY; MODELS;

D O I：

10.1016/j.cplett.2009.04.025

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

We have recently shown that the water entropy is the key quantity in elucidating the folding/unfolding mechanisms for proteins. Here we consider thermal denaturation. The water-entropy gain upon the transition from the random-coil state to the native structure is calculated for some representative proteins by employing the angle-dependent integral equation theory combined with the multipolar water model and the morphometric approach. It is found that the water-entropy gain at 25 degrees C divided by the number of residues is a good measure of the thermal stability. A protein with a larger value of this measure tends to have a higher denaturation temperature. (C) 2009 Elsevier B. V. All rights reserved.

引用

页码：190 / 194

页数：5

共 32 条

[1] The factors governing the thermal stability of frataxin orthologues: How to increase a protein's stability [J].