Thermodynamic study of the binding of calcium and magnesium ions with myelin basic protein using the extended
G Rezaei Behbehani1, A A Saboury, A Divsalar
1Chemistry Department, Imam Khomeini International University, Qazvin, Iran. grb402003@yahoo.com
Abstract:
The interaction of myelin basic protein (MBP) from the bovine central nervous system with Ca2+ and Mg2+ ions, named as M2+, was studied by isothermal titration calorimetry at 27 degrees C in aqueous solution. The extended solvation model was used to reproduce the enthalpies of MBP+M2+ interactions. The solvation parameters recovered from the extended 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 noninteracting binding sites for Ca2+ and Mg2+ ions.
Related Concept Videos
The Equilibrium Binding Constant and Binding Strength
The Equilibrium Binding Constant and Binding Strength
The Debye–Hückel Theory of Electrolyte Solutions
Calmodulin-dependent Signaling
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
Theory of Strong Electrolytes
The Resting Membrane Potential

