A knowledge-based potential highlights unique features of membrane α-helical and β-barrel protein insertion and folding
A knowledge-based potential highlights unique features of membrane α-helical and β-barrel protein insertion and folding
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DOI：
10.1002/pro.758
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发表时间：
2012-01-01
期刊：
影响因子：
8
通讯作者：
Nanda, Vikas
中科院分区：
文献类型：
--
作者：
Hsieh, Daniel;Davis, Alexander;Nanda, Vikas
外膜β -桶蛋白与a-螺旋内膜蛋白在脂质环境、二级结构、折叠和插入过程等方面存在差异。我们有理由认为外膜蛋白可能含有与它们的折叠和插入行为相关的初级序列信息。在之前的工作中，我们推导出了a-螺旋内膜蛋白的深度依赖插入电位E-z。我们已经生成了TM β -桶蛋白的等效电位。这两种电位之间的相似性和差异性提供了对-桶膜蛋白折叠和插入的独特方面的见解。这种电位可以预测膜内的取向和识别参与分子间相互作用的功能残基。
Outer membrane beta-barrel proteins differ from a-helical inner membrane proteins in lipid environment, secondary structure, and the proposed processes of folding and insertion. It is reasonable to expect that outer membrane proteins may contain primary sequence information specific for their folding and insertion behavior. In previous work, a depth-dependent insertion potential, E-z, was derived for a-helical inner membrane proteins. We have generated an equivalent potential for TM beta-barrel proteins. The similarities and differences between these two potentials provide insight into unique aspects of the folding and insertion of beta-barrel membrane proteins. This potential can predict orientation within the membrane and identify functional residues involved in intermolecular interactions.