静电排斥对蛋白质二聚化影响的修正值
Allowance for effects of electrostatic repulsion on protein dimerization.
作者信息
Agapow P M, Winzor D J
机构信息
Department of Biochemistry, University of Queensland, St. Lucia, Australia.
出版信息
Biochim Biophys Acta. 1988 Mar 23;953(2):197-200. doi: 10.1016/0167-4838(88)90024-6.
A simple procedure for assessing the extent of electrostatic effects on protein dimerization is described and illustrated by application to published results on the ionic strength dependence of the dimerization constant for alpha-chymotrypsin at pH 4 (Aune, K.C., Goldsmith, L.C. and Timasheff, S.N. (1971) Biochemistry 10, 1617-1622). From the analysis it is concluded that the inverse dependence of alpha-chymotrypsin dimerization upon ionic strength is predominantly a general electrostatic effect, rather than a consequence of repulsion between two specific charged residues on the adjacent monomers comprising dimer.
本文描述了一种评估静电作用对蛋白质二聚化影响程度的简单方法，并通过应用于已发表的关于pH 4时α-胰凝乳蛋白酶二聚化常数的离子强度依赖性的结果进行了说明（奥恩，K.C.，戈德史密斯，L.C.和蒂马斯谢夫，S.N.（1971年）《生物化学》10，1617 - 1622）。通过分析得出结论，α-胰凝乳蛋白酶二聚化对离子强度的反比依赖性主要是一种普遍的静电效应，而不是由构成二聚体的相邻单体上两个特定带电残基之间的排斥作用导致的。
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