MODELS FOR THE STRUCTURE OF OUTER-MEMBRANE PROTEINS OF ESCHERICHIA-COLI DERIVED FROM RAMAN-SPECTROSCOPY AND PREDICTION METHODS
MODELS FOR THE STRUCTURE OF OUTER-MEMBRANE PROTEINS OF ESCHERICHIA-COLI DERIVED FROM RAMAN-SPECTROSCOPY AND PREDICTION METHODS
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DOI：
10.1016/0022-2836(86)90292-5
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发表时间：
1986-07-20
影响因子：
5.6
通讯作者：
JAHNIG, F
中科院分区：
文献类型：
--
作者：
VOGEL, H;JAHNIG, F
通过拉曼光谱测定了在脂质膜中重构的孔蛋白、麦芽孔蛋白和OmpA蛋白的二级结构。这三种蛋白质具有相似的结构，由50至60%的β-链，约20% β-转向，并且小于15% α-螺旋。采用解释两亲性β-环的结构预测方法，链，折叠模型的孔蛋白和OmpA蛋白的片段纳入膜。在该模型中，OmpA片段由八个两亲性跨膜β-形成β的链-每桶类似地，孔蛋白折叠成十个两亲性跨膜β-葡聚糖。位于三聚体表面朝向脂质的链和内部的八个主要亲水链。
The secondary structure of porin, maltoporin and OmpA protein reconstituted in lipid membranes is determined by Raman spectroscopy. The three proteins have similar structures consisting of 50 to 60% .beta.-strand, about 20% .beta.-turn, and less than 15% .alpha.-helix. Employing a method for structural prediction that accounts for amphipathic .beta.-strands, folding models are developed for porin and for the segment of OmpA protein incorporated into the membrane. In the model, the OmpA fragment consists of eight amphipathic membrane-spanning .beta.-strands that form a .beta.-barrel. Similarly, porin is folded into ten amphipathic membrane-spanning .beta.-strands that are located at the surface of the trimer towards the lipids and eight predominantly hydrophilic strands in the interior.