Abstract
The interaction of myelin basic protein (MBP) from the bovine central nervous system with divalent calcium ion was studied by isothermal titration calorimetry at 27 °C in aqueous solution. The extended solvation model was used to reproduce the enthalpies of Ca2+-MBP interaction over the whole range of Ca2+ 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 two identical and non-interacting binding sites for Ca2+ ions. The association equilibrium constant is 0.021 μmol⋅dm−3. The molar enthalpy of binding is ΔH=−15.10 kJ⋅mol−1.
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