THE TEMPERATURE-INDUCED DENATURATION OF SMALL GLOBULAR-PROTEINS AS A FIRST-ORDER PHASE-TRANSITION OF CRYSTAL MOLECULES

被引：4

作者：

GRAZIANO, G ^{[1
]}

BARONE, G ^{[1
]}

CATANZANO, F ^{[1
]}

RICCIO, A ^{[1
]}

机构：

[1] UNIV NAPLES,DEPT CHEM,I-80134 NAPLES,ITALY

来源：

JOURNAL OF THERMAL ANALYSIS | 1995年 / 44卷 / 04期

关键词：

CRYSTAL MOLECULES; PHASE TRANSITION; PROTEINS;

D O I：

10.1007/BF02547263

中图分类号：

O414.1 [热力学];

学科分类号：

摘要：

A general feature of temperature-induced reversible denaturation of small globular proteins is its all-or-none character. This strong cooperativity leads to think that protein molecules, possessing only two accessible thermodynamic states, the native and the denatured one, resemble 'crystal molecules' that melt at raising temperature. An analysis, grounded on mean field theory, allows to conclude that the two-state transition is a first-order phase transition. The implication of this conclusion are briefly discussed.

引用

页码：765 / 775

页数：11

共 50 条

[1]

ALLEGRA G, 1987, GAZZ CHIM ITAL, V117, P99

[2] POLYMER COLLAPSE IN DILUTE-SOLUTION - EQUILIBRIUM AND DYNAMICAL ASPECTS [J].