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首页> 外文期刊>Biochemistry >Anomalous orientation-dependent effective pair interaction among histidine and other amino acid residues in metalloproteins: Breakdown of the hydropathy scale index
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Anomalous orientation-dependent effective pair interaction among histidine and other amino acid residues in metalloproteins: Breakdown of the hydropathy scale index

机译：组氨酸与金属蛋白中其他氨基酸残基之间异常的定向依赖性有效对相互作用：亲水性量表指数的分解

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Hydropathy scale is widely used to obtain a measure of the effective interaction between any two amino acid residues in proteins and is based on the assumption that attraction between two hydrophobic groups and repulsion between hydrophilic groups (in water) can be translated straightforwardly to protein environment. Here we employ a recently developed statistical mechanical approach combined with the Protein Data Bank to obtain both distance- and orientation-dependent potential of mean force (ODPMF). This allowed Lis to explore effective pair potential among many amino acid residues and to examine the validity of the hydropathy scale in modeling the interaction among amino acid residues. We find that in some cases, like Phe-Phe and Lys-Lys, the hydropathy scale approach is largely obeyed. However, we also observe many unexpected pair interactions which defy the trend given by published hydropathy scales. An example of the former is the arginine-arginine (Arg-Arg) pair interaction which is found to be strongly and surprisingly attractive at short separation, even though it is the most hydrophilic residue. Here the head-to-head (see text) interaction is also stabilized. Tryptophan residues also exhibit strong attractive interaction. Equally important, we find strong influence of metal in determining effective interaction among the amino acid residues. It is the behavior of the histidine (His) which is found to be the most unusual. It exhibits a strong attractive interaction with itself which gets significantly enhanced in metalloproteins. These results highlight the important (sometime hidden) role of metals in protein structure and folding.
机译：亲水性标度被广泛用于获得蛋白质中任何两个氨基酸残基之间有效相互作用的量度，并且基于以下假设：两个疏水基团之间的吸引力和亲水性基团（在水中）之间的排斥力可以直接转化为蛋白质环境。在这里，我们采用了最近开发的统计机械方法，结合蛋白质数据库来获得平均力（ODPMF）的距离和方向相关电位。这使Lis可以探索许多氨基酸残基之间的有效配对电位，并可以检验亲水性量表在模拟氨基酸残基之间相互作用时的有效性。我们发现，在某些情况下，如Phe-Phe和Lys-Lys，大多采用亲水性量表法。但是，我们还观察到许多意外的配对相互作用，这与已发表的水肿量表给出的趋势相反。前者的一个例子是精氨酸-精氨酸（Arg-Arg）对相互作用，尽管它是最亲水的残基，但在短距离分离时仍具有强大且出人意料的吸引力。在这里，头对头（参见文本）的交互也得以稳定。色氨酸残基也表现出强烈的吸引力相互作用。同样重要的是，我们发现金属在确定氨基酸残基之间的有效相互作用方面具有强大的影响力。组氨酸（His）的行为被发现是最不寻常的。它与自身表现出很强的吸引力相互作用，金属蛋白得到显着增强。这些结果突出了金属在蛋白质结构和折叠中的重要作用（有时是隐藏的）。

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