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首页> 外文期刊>Biophysical Journal >Aggregation of model membrane proteins, modulated by hydrophobic mismatch, membrane curvature, and protein class.
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Aggregation of model membrane proteins, modulated by hydrophobic mismatch, membrane curvature, and protein class.

机译:模型膜蛋白的聚集,受疏水错配,膜曲率和蛋白类别的调节。

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Aggregation of transmembrane proteins is important for many biological processes, such as protein sorting and cell signaling, and also for in vitro processes such as two-dimensional crystallization. We have used large-scale simulations to study the lateral organization and dynamics of lipid bilayers containing multiple inserted proteins. Using coarse-grained molecular dynamics simulations, we have studied model membranes comprising approximately 7000 lipids and 16 identical copies of model cylindrical proteins of either alpha-helical or beta-barrel types. Through variation of the lipid tail length and hence the degree of hydrophobic mismatch, our simulations display levels of protein aggregation ranging from negligible to extensive. The nature and extent of aggregation are shown to be influenced by membrane curvature and the shape or orientation of the protein. Interestingly, a model beta-barrel protein aggregates to form one-dimensional strings within the bilayer plane, whereas a model alpha-helical bundle forms two-dimensional clusters. Overall, it is clear that the nature and extent of membrane protein aggregation is dependent on several aspects of the proteins and lipids, including hydrophobic mismatch, protein class and shape, and membrane curvature.
机译:跨膜蛋白的聚集对于许多生物学过程(例如蛋白分选和细胞信号转导)以及体外过程(例如二维结晶)都非常重要。我们已经使用大规模模拟来研究包含多个插入蛋白的脂质双层的横向组织和动力学。使用粗粒度的分子动力学模拟,我们研究了包含约7000种脂质和16个相同拷贝的α-螺旋或β-桶型模型圆柱形蛋白质的模型膜。通过改变脂类尾巴的长度,从而改变疏水性错配的程度,我们的模拟显示蛋白质聚集的水平范围可以忽略不计。聚集的性质和程度显示受膜曲率和蛋白质形状或方向的影响。有趣的是,模型β-桶状蛋白质聚集在双层平面内形成一维字符串,而模型α-螺旋束形成二维簇。总体而言,很明显,膜蛋白聚集的性质和程度取决于蛋白和脂质的多个方面,包括疏水性错配,蛋白类别和形状以及膜曲率。

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