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The interaction of the myelin basic protein (MBP) from the bovine central nervous system with divalent magnesium ion was studied by isothermal titration calorimetry at 27°C in aqueous solution. A simple rapid method for determination of the dissociation binding constants for Mg 2+ -MBP interaction was introduced using the isothermal titration calometric data. The binding isotherm for Mg 2+ -MBP interaction is easily obtained by carrying out a titration calorimetric experiment using only one set of concentrations of MBP. There are two identical independent intrinsic association constants equal to 0.021 μmol·L −1 in the first-and second-binding sites, respectively.

The interaction of myelin basic protein (MBP) from bovine central nervous system with divalent calcium ion was studied by isothermal titration calorimetry at 27 o C in aqueous solution. The extended solvation model was used to reproduce the enthalpies of Co 2+ -MBP interaction over the whole Co 2+ concentrations. The solvation parameters recovered from the solvation model were attributed to the structural change of MBP due to the metal ion interaction. It was found that there is a set of three identical and noninteracting binding sites for Co 2+ ions.The association equilibrium constant is 0.015 μM −1. The molar enthalpy of binding is ΔH = −14.60 kJ mol −1.