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首页> 外文期刊>Journal of Molecular Biology >COMPLEX SALT BRIDGES IN PROTEINS - STATISTICAL ANALYSIS OF STRUCTURE AND FUNCTION
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COMPLEX SALT BRIDGES IN PROTEINS - STATISTICAL ANALYSIS OF STRUCTURE AND FUNCTION

机译：蛋白质中的复杂盐桥-结构和功能的统计分析

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We developed an algorithm to analyze the distribution and geometry of simple and complex salt bridges in 94 proteins selected from the Protein Data Bank. In this study, the term ''salt bridging'' denotes both non-bonded and hydrogen-bonded paired electrostatic interactions between acidic carboxyl groups and basic amino groups in single or adjacent protein chains. We defined complex salt bridges as those joining more than two charged residues, including Asp, Glu, Lys and Arg, and excluding His. The survey related the following special features of complex salt bridges. (1) The abundance of complex salt bridges is high; one-third of all residues participating in salt-bridge formation were part of complex salt bridges. (2) The geometry of the interaction between acidic and basic residues is very similar in simple and complex salt bridges. Adding one residue to a simple interaction represents a minor change in the geometry but provides the molecule with a more complex interaction, a phenomenon that may explain the cooperative effect of salt bridges in proteins. Such moderate changes in salt-bridge networks can be generated stepwise and reversibly without trapping the protein in a local energetic minimum. (3) One important role of complex salt bridges is connecting protein subunits or joining two secondary structures to form quaternary structures, where they can connect as many as five secondary structure units. (4) Arginine serves as a key connector and/or a branching unit because its geometry allows three possible directions of interactions. The information gained from this study of complex salt bridges should enhance the understanding of protein structure. (C) 1995 Academic Press Limited [References: 29]
机译：我们开发了一种算法来分析从蛋白质数据库中选择的94种蛋白质中简单和复杂盐桥的分布和几何形状。在这项研究中，术语“盐桥联”表示单个或相邻蛋白质链中酸性羧基和碱性氨基之间的未键合和氢键配对的静电相互作用。我们将复杂的盐桥定义为那些连接两个以上带电残基的盐桥，包括Asp，Glu，Lys和Arg，但不包括His。调查涉及复杂盐桥的以下特殊功能。 （1）复杂的盐桥丰度高;参与盐桥形成的所有残基的三分之一是复杂盐桥的一部分。 （2）在简单和复杂的盐桥中，酸性残基和碱性残基之间相互作用的几何形状非常相似。在简单的相互作用中添加一个残基表示几何形状的微小变化，但为分子提供了更为复杂的相互作用，这种现象可以解释蛋白质中盐桥的协同作用。盐桥网络的这种适度变化可以逐步且可逆地生成，而不会将蛋白质陷于局部高能最小值。 （3）复杂盐桥的重要作用是连接蛋白质亚基或连接两个二级结构以形成四级结构，它们最多可连接五个二级结构单元。 （4）精氨酸用作键连接器和/或分支单元，因为其几何形状允许相互作用的三个可能方向。从复杂盐桥的这项研究中获得的信息应增强对蛋白质结构的了解。 （C）1995 Academic Press Limited [参考：29]

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