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首页> 外文期刊>Biochemistry >Role of helix-helix interactions in assembly of the bacteriorhodopsin lattice.
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Role of helix-helix interactions in assembly of the bacteriorhodopsin lattice.

机译：螺旋-螺旋相互作用在细菌视紫红质晶格组装中的作用。

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摘要

The purple membrane of Halobacterium salinarium is a two-dimensional lattice of lipids and the integral membrane protein bacteriorhodopsin (BR). To determine whether helix-helix interactions within the membrane core stabilize this complex, we substituted amino acid residues at the helix-helix interface between BR monomers and examined the assembly of the protein into the lattice. Lattice assembly was demonstrated to fit a cooperative self-assembly model that exhibits a critical concentration in vivo. Using this model as the basis for a quantitative assay of lattice stability, bulky substitutions at the helix-helix interface between BR monomers within the membrane core were shown to be destabilizing, probably due to steric clash. Ala substitutions of two residues at the helix-helix interface also reduced stability, suggesting that the side chains of these residues participate in favorable van der Waals packing interactions. However, the stabilizing interactions were restricted to a small region of the interface, and most of the substitutions had little effect. Thus, the contribution of helix-helix interactions to lattice stability appears limited, and favorable interactions between other regions of neighboring BR monomers or between BR and lipid molecules must also contribute.
机译：盐杆菌盐渍膜的紫色膜是脂质和完整膜蛋白细菌视紫红质（BR）的二维晶格。为了确定膜核心中的螺旋-螺旋相互作用是否稳定该复合物，我们在BR单体之间的螺旋-螺旋界面处取代了氨基酸残基，并检查了蛋白质组装成晶格的情况。晶格组装被证明适合于在体内展现出临界浓度的协作自组装模型。使用该模型作为晶格稳定性定量分析的基础，膜核内BR单体之间的螺旋-螺旋界面处的大量取代被证明不稳定，这可能是由于空间碰撞所致。螺旋-螺旋界面上两个残基的丙氨酸取代也降低了稳定性，表明这些残基的侧链参与了有利的范德华堆积相互作用。但是，稳定化相互作用仅限于界面的一小部分，大多数取代作用不大。因此，螺旋-螺旋相互作用对晶格稳定性的贡献似乎是有限的，并且相邻BR单体的其他区域之间或BR与脂质分子之间的有利相互作用也必须起作用。

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