FORCES AND FACTORS THAT CONTRIBUTE TO THE STRUCTURAL STABILITY OF MEMBRANE-PROTEINS

被引:130
作者
HALTIA, T
FREIRE, E
机构
[1] JOHNS HOPKINS UNIV, DEPT BIOL, BALTIMORE, MD 21218 USA
[2] JOHNS HOPKINS UNIV, CTR BIOCALORIMETRY, BALTIMORE, MD 21218 USA
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS | 1995年 / 1228卷 / 01期
关键词
CALORIMETRY; THERMAL STABILITY; BACTERIORHODOPSIN; CYTOCHROME OXIDASE; BAND; 3; PROTEIN; PHOTOSYSTEM II;
D O I
10.1016/0005-2728(94)00161-W
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
While a considerable amount of literature deals with the structural energetics of water-soluble proteins, relatively little is known about the forces that determine the stability of membrane proteins. Similarly, only a few membrane protein structures are known at atomic resolution, although new structures have recently been described. In this article, we review the current knowledge about the structural features of membrane proteins. We then proceed to summarize the existing literature regarding the thermal stability of bacteriorhodopsin, cytochrome-e oxidase, the band 3 protein, Photosystem II and porins. We conclude that a fundamental difference between soluble and membrane proteins is the high thermal stability of intrabilayer secondary structure elements in membrane proteins. This property manifests itself as incomplete unfolding, and is reflected in the observed low enthalpies of denaturation of most membrane proteins. By contrast, the extramembranous parts of membrane proteins may behave much like soluble proteins. A brief general account of thermodynamics factors that contribute to the stability of water soluble and membrane proteins is presented.
引用
收藏
页码:1 / 27
页数:27
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