Vogel H, Jähnig F
J Mol Biol. 1986 Jul 20;190(2):191-9. doi: 10.1016/0022-2836(86)90292-5.
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.
通过拉曼光谱法测定了脂质膜中重组的孔蛋白、麦芽寡糖孔蛋白和外膜蛋白A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%的β转角和少于15%的α螺旋组成。采用一种考虑两亲性β链的结构预测方法，构建了孔蛋白和整合到膜中的外膜蛋白A片段的折叠模型。在该模型中，外膜蛋白A片段由八个形成β桶的两亲性跨膜β链组成。同样，孔蛋白折叠成十个位于三聚体表面朝向脂质的两亲性跨膜β链和八个主要位于内部的亲水性链。
