Membrane protein function and stability has been shown to be dependent on the lipid environment. Recently, we developed a high-throughput computational approach for the prediction of membrane protein/lipid interactions. In the current study, we enhanced this approach with the addition of a new measure of the distortion caused by membrane proteins on a lipid bilayer. This is illustrated by considering the effect of lipid tail length and headgroup charge on the distortion caused by the integral membrane proteins MscS and FLAP, and by the voltage sensing domain from the channel KvAP. Changing the chain length of lipids alters the extent but not the pattern of distortion caused by MscS and FLAP; lipid headgroups distort in order to interact with very similar but not identical regions in these proteins for all bilayer widths investigated. Introducing anionic lipids into a DPPC bilayer containing the KvAP voltage sensor does not affect the extent of bilayer distortion.

中文翻译：

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CGDB：通过粗粒分子动力学模拟的膜蛋白/脂质相互作用的数据库。

膜蛋白的功能和稳定性已显示取决于脂质环境。最近，我们开发了一种预测膜蛋白/脂质相互作用的高通量计算方法。在当前的研究中，我们通过增加一种新的措施来增强这种方法，该措施可以测量脂质双层上膜蛋白引起的变形。通过考虑脂质尾巴长度和头基电荷对整合膜蛋白MscS和FLAP以及通道KvAP的电压感应域引起的畸变的影响，可以说明这一点。改变脂质的链长不会改变由MscS和FLAP引起的变形的程度，但不会改变。对于所研究的所有双层宽度，脂质头基都扭曲以与这些蛋白质中非常相似但不完全相同的区域相互作用。