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首页> 外文期刊>Protoplasma: An International Journal of Cell Biology >Contribution of cation-pi interactions to the stability of Sm/LSm oligomeric assemblies
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Contribution of cation-pi interactions to the stability of Sm/LSm oligomeric assemblies

机译：阳离子-pi相互作用对Sm / LSm低聚物组装体稳定性的贡献

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In this work, we have analyzed the influence of cation-pi interactions to the stability of Sm/LSm assemblies and their environmental preferences. The number of interactions formed by arginine is higher than lysine in the cationic group, while histidine is comparatively higher than phenylalanine and tyrosine in the pi group. Arg-Tyr interactions are predominant among the various pairs analyzed. The furcation level of multiple cation-pi interactions is much higher than that of single cation-pi interactions in Sm/LSm interfaces. We have found hot spot residues forming cation-pi interactions, and hot spot composition is similar for all aromatic residues. The Arg-Phe pair has the strongest interaction energy of -8.81 kcal mol(-1) among all the possible pairs of amino acids. The extent of burial of the residue side-chain correlates with the Delta Delta G of binding for residues in the core and also for hot spot residues cation-pi bonded across the interface. Secondary structure of the cation-pi residues shows that Arg and Lys preferred to be in strand. Among the pi residues, His prefers to be in helix, Phe prefers to be in turn, and Tyr prefers to be in strand. Stabilization centers for these proteins showed that all the five residues found in cation-pi interactions are important in locating one or more of such centers. More than 50 % of the cation-pi interacting residues are highly conserved. It is likely that the cation-pi interactions contribute significantly to the overall stability of Sm/LSm proteins.
机译：在这项工作中，我们分析了阳离子-pi相互作用对Sm / LSm组件的稳定性及其环境偏好的影响。精氨酸形成的相互作用数在阳离子基团中高于赖氨酸，而组氨酸在pi基团中则高于苯丙氨酸和酪氨酸。在所分析的各种对中，Arg-Tyr相互作用占主导。 Sm / LSm界面中多个阳离子-pi相互作用的分叉水平远高于单个阳离子-pi相互作用的分叉水平。我们发现热点残基形成阳离子-pi相互作用，并且所有芳香族残基的热点组成均相似。在所有可能的氨基酸对中，Arg-Phe对具有最强的相互作用能-8.81 kcal mol（-1）。残基侧链的埋藏程度与核心残基以及结合在界面上的阳离子pi结合的热点残基的结合Delta Delta G相关。阳离子-pi残基的二级结构表明，Arg和Lys优选成对存在。在pi残基中，His倾向于呈螺旋状，Phe倾向于呈螺旋状，而Tyr则倾向于呈螺旋状。这些蛋白质的稳定化中心表明，在阳离子-π相互作用中发现的所有五个残基对定位一个或多个此类中心都很重要。超过50％的阳离子-pi相互作用残基高度保守。阳离子-pi相互作用可能对Sm / LSm蛋白的整体稳定性有重要贡献。

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