Application of an extended solvation theory to study on the binding of magnesium ion with myelin basic protein
Application of an extended solvation theory to study on the binding of magnesium ion with myelin basic protein
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DOI：
10.1007/s10973-007-8674-7
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发表时间：
2008-08-01
影响因子：
4.4
通讯作者：
Abedini, A.
中科院分区：
文献类型：
--
作者：
Behbehani, G. Rezaei;Saboury, A. A.;Abedini, A.
采用等温滴定量热法（ITC）研究了27 ℃下牛中枢神经系统髓鞘碱性蛋白（MBP）与二价镁离子（Mg ~（2+））相互作用的结合特性。扩展的溶剂化模型被用来再现整个Mg 2+浓度的Mg 2 +-MBP相互作用的光谱。结果发现，有一组的两个相同的和非相互作用的结合位点的Mg 2+离子。解离平衡常数K-d=45.5 μ M。两个位点结合位点的摩尔焓相同; Δ H= -15.24 kJ mol（-1）。从溶剂化模型恢复的溶剂化参数归因于MBP的结构变化，由于金属离子的相互作用。
Binding properties of myelin basic protein (MBP) from bovine central nervous system due to the interaction by divalent magnesium ion (Mg2+) was investigated at 27 degrees C in aqueous solution using isothermal titration calorimetry (ITC) technique. An extended solvation model was used to reproduce the enthalpies of Mg2+-MBP interaction over the whole Mg2+ concentrations. It was found that there is a set of two identical and noninteracting binding sites for Mg2+ ions. The dissociation equilibrium constant is K-d=45.5 mu M. The molar enthalpy of binding site is identical for both sites; Delta H= -15.24 kJ mol(-1). The solvation parameters recovered from the solvation model were attributed to the structural change of MBP due to the metal ion interaction.