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Protein patterns at lipid bilayer junctions.

机译:脂质双层连接处的蛋白质模式。

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We introduce a simple intermembrane junction system in which to explore pattern and structure formation by membrane-bound proteins. The junction consists of a planar lipid bilayer to which one species of protein (an IgG antibody) is bound, forming a 2D, compressible fluid. Upon the adhesion of a second lipid bilayer, the formerly uniformly distributed proteins rapidly reorganize into patterns of dense and sparse zones. Using a combination of complementary imaging techniques (fluorescence microscopy, fluorescence interference contrast microscopy, and fluorescence resonance energy transfer), we reconstruct the 3D structure of these intermembrane patterns with nanometer-scale topographic resolution, revealing the orientation of the proteins. The patterns form as the rapid bilayer-bilayer adhesion, often radiating outward from an initial, circular contact site, pushes aside the antibodies, sweeping them into areas of high density and clearing low-density regions. Coarsening of these local features is energetically costly and therefore kinetically trapped; the patterns do not change over tens of minutes. These studies demonstrate that membrane mechanical forces alone, i.e., in the absence of specific biochemical interactions, can drive microm-scale organization of membrane proteins.
机译:我们介绍了一个简单的膜间连接系统,在其中探索膜结合蛋白形成的模式和结构。连接处由平面脂质双层组成,一种蛋白质(IgG抗体)结合到该脂质双层上,形成2D可压缩流体。在第二个脂质双层粘附后,以前均匀分布的蛋白质迅速重组为密集和稀疏区域的模式。通过使用互补成像技术(荧光显微镜,荧光干涉对比显微镜和荧光共振能量转移)的组合,我们以纳米级的地形分辨率重建了这些膜间模式的3D结构,揭示了蛋白质的方向。图案形成为快速的双层-双层粘附,通常从初始的圆形接触点向外辐射,将抗体推开,将其扫入高密度区域并清除低密度区域。这些局部特征的粗化在能量上是昂贵的,因此在动力学上是被困住的。模式不会在数十分钟内改变。这些研究表明,单独的膜机械力,即在没有特定生化相互作用的情况下,可以驱动微米级的膜蛋白组织。

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