Cluster formation of membrane proteins is a crucial event in many vital cellular processes. Here, we present a thorough examination of the oligomerisation ability of membrane proteins with different geometries. By means of mesoscopic membrane simulations we show that lipid-mediated interactions between proteins depend both on the shape of the hydrophobic domain of the proteins and on their hydrophobic mismatch. Based on that, we find that protein interactions can be either attractive or repulsive, depending on the characteristic bilayer perturbations induced by the proteins. The influence of these perturbations is quantified via the associated potential of mean force. Such geometry-dependent interactions are likely to fine-tune protein oligomerization events during cellular processes, for example signal transduction or protein sorting.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据