A study of the membrane-water interface region of membrane proteins
A study of the membrane-water interface region of membrane proteins
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DOI：
10.1016/j.jmb.2004.11.036
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发表时间：
2005-02-11
影响因子：
5.6
通讯作者：
Elofsson, A
中科院分区：
文献类型：
--
作者：
Granseth, E;von Heijne, G;Elofsson, A
螺旋膜蛋白最显著的结构特征是其长长的跨膜螺旋。然而，在膜蛋白结构的统计研究中，在位于膜-水界面区域的蛋白质中发现了其他结构元素，这些结构元素在很大程度上被忽略了。在这里，我们发现该区域富含不规则结构和与膜表面大致平行的界面螺旋，而β链非常罕见。界面螺旋、位于界面区域的部分跨膜螺旋和不规则结构之间的平均氨基酸组成不同。在这个区域，疏水和芳香残基倾向于指向膜，而带电/极性残基倾向于远离膜。因此，与膜的中心碳氢化合物核心和周围的水相相比，界面区域对蛋白质结构施加了不同的约束。(C) 2004 Elsevier Ltd.版权所有。
The most conspicuous structural characteristic of the alpha-helical membrane proteins is their long transmembrane alpha-helices. However, other structural elements, as yet largely ignored in statistical studies of membrane protein structure, are found in those parts of the protein that are located in the membrane-water interface region. Here, we show that this region is enriched in irregular structure and in interfacial helices running roughly parallel with the membrane surface, while beta-strands are extremely rare. The average amino acid composition is different between the interfacial helices, the parts of the transmembrane helices located in the interface region, and the irregular structures. In this region, hydrophobic and aromatic residues tend to point toward the membrane and charged/polar residues tend to point away from the membrane. The interface region thus imposes different constraints on protein structure than do the central hydrocarbon core of the membrane and the surrounding aqueous phase. (C) 2004 Elsevier Ltd. All rights reserved.