(1) Chemistry Department, Imam Khomeini International University, Qazvin, Iran;(2) Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran;(3) Chemistry Department, Payam Noor University, Abhar, Iran
Abstract:
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°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 Kd=45.5 μM. The molar enthalpy of binding site is identical for both sites; ΔH=−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.