单分子蛋白质表面暴露的氨基酸残基决定了水两相体系中的分配

Kristina Berggren , Alejandro Wolf , Juan A. Asenjo , Barbara A. Andrews , Folke Tjerneld
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引用次数: 82

摘要

不同的氨基酸残基如何促成和影响蛋白质表面的性质是非常有趣和重要的。在水两相体系中分配有潜力作为一种快速和简单的方法来研究蛋白质的表面性质。研究了八种结构确定的单体蛋白表面暴露氨基酸残基对其分配的影响。通过计算机程序“表面性质图形表示与分析”(GRASP)对蛋白质的表面暴露残留物进行了表征,并将其分为两种EO30PO70 -葡聚糖水相体系,仅聚合物浓度不同(体系1:6.8% EO30PO70, 7.1%葡聚糖;体系II: 9% EO30PO70, 9%葡聚糖)。我们首次表明,不同单体蛋白的分配行为可以通过表面暴露的氨基酸残基的差异来描述。发现残基对分配系数的贡献最好地表征为两水相体系中的肽分配。与文献中可用的疏水性尺度相比,对于只含有一种残基的不同长度的肽,每个氨基酸的贡献用log K对肽链长度的曲线斜率来表征。结果还表明,每个氨基酸的贡献与蛋白质的总表面和表面上的其他残基有关。对体系I和体系II实现的表面疏水性计算,其log K与计算的疏水性值的线性关系的相关系数分别为0.961和0.949。为了研究不同氨基酸对配分系数的影响,根据它们的共同特征:是否存在芳香基团、是否存在长脂肪链或是否存在电荷,将它们分为几类。利用这些基团,可以确定芳香残基对分配系数的影响最大,优先考虑体系上部的EO30PO70相;另一方面,蛋白质表面带电氨基酸的存在增强了蛋白质向右旋糖酐相的分配。同样值得注意的是,随着聚合物浓度的增加,eo30po70 -葡聚糖体系对表面暴露残留物的灵敏度增加。因此,单体蛋白的分配系数可以通过其表面暴露的氨基酸残基来预测,该系统也可以用于一般的单体蛋白表面表征。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
The surface exposed amino acid residues of monomeric proteins determine the partitioning in aqueous two-phase systems

It is of great interest and importance how different amino acid residues contribute to and affect the properties of a protein surface. Partitioning in aqueous two-phase systems has the potential to be used as a rapid and simple method for studying the surface properties of proteins. The influence on partitioning of the surface exposed amino acid residues of eight structurally determined monomeric proteins has been studied. The proteins were characterized in terms of surface exposed residues with a computer program, Graphical Representation and Analysis of Surface Properties (GRASP), and partitioned in two EO30PO70–dextran aqueous two-phase systems, only differing in polymer concentrations (system I: 6.8% EO30PO70, 7.1% dextran; system II: 9% EO30PO70, 9% dextran). We show for the first time that the partitioning behaviour of different monomeric proteins can be described by the differences in surface exposed amino acid residues. The contribution to the partition coefficient of the residues was found to be best characterized by peptide partitioning in the aqueous two-phase system. Compared to hydrophobicity scales available in the literature, each amino acid contribution is characterized by the slope given by the graph of log K against peptide chain length, for peptides of different length containing only one kind of residue. It was also shown that each amino acid contribution is relative to the total protein surface and the other residues on the surface. Surface hydrophobicity calculations realized for systems I and II gave respectively correlation coefficients of 0.961 and 0.949 for the linear relation between log K and calculated hydrophobicity values. To study the effect on the partition coefficient of different amino acids, they were grouped into classes according to common characteristics: the presence of an aromatic group, a long aliphatic chain or the presence of charge. Using these groups it was possible to confirm that aromatic residues have the strongest effect on the partition coefficient, giving preference to the upper EO30PO70 phase of the system; on the other hand the presence of charged amino acids on the protein surface enhances the partition of the protein to the lower dextran phase. It is also important to note that the sensitivity of the EO30PO70–dextran system for the surface exposed residues was increased by increasing the polymer concentrations. The partition coefficient of a monomeric protein can thus be predicted from its surface exposed amino acid residues and the system can also be used to characterize protein surfaces of monomeric proteins in general.

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