HYDROPHOBIC ORGANIZATION OF MEMBRANE-PROTEINS
HYDROPHOBIC ORGANIZATION OF MEMBRANE-PROTEINS
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DOI：
10.1126/science.2667138
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发表时间：
1989-08-04
期刊：
影响因子：
56.9
通讯作者：
EISENBERG, D
中科院分区：
文献类型：
--
作者：
REES, DC;DEANTONIO, L;EISENBERG, D
球状红杆菌光合作用反应中心跨膜区的膜暴露残基比埋藏的内部残基更疏水性。这种疏水组织与水溶性蛋白质相反。然而，膜和水溶性蛋白质内部和表面残基的相对极性并不简单地反转。膜蛋白和水溶性蛋白内部残基的疏水性相当，而膜蛋白双层暴露残基的疏水性比膜蛋白内部残基的疏水性强，而水溶性蛋白的水暴露残基的亲水性强于膜蛋白的内部残基。描述了一种基于同源序列中残基替换的周期性的序列分析方法，该方法将从反应中心的已知原子结构得出的结论扩展到更广泛的假定跨膜螺旋序列的数据库。
Membrane-exposed residues are more hydrophobic than buried interior residues in the transmembrane regions of the photosynthetic reaction center from Rhodobacter sphaeroides. This hydrophobic organization is opposite to that of water-soluble proteins. The relative polarities of interior and surface residues of membrane and water soluble proteins are not simply reversed, however. The hydrophobicities of interior residues of both membrane and water-soluble proteins are comparable, whereas the bilayer-exposed residues of membrane proteins are more hydrophobic than the interior residues, and the aqueous-exposed residues of water-soluble proteins are more hydrophilic than the interior residues. A method of sequence analysis is described, based on the periodicity of residue replacement in homologous sequences, that extends conclusions derived from the known atomic structure of the reaction center to the more extensive database of putative transmembrane helical sequences.