title: Thermodynamic study of the binding of calcium and magnesium ions with myelin basic protein using the extended solvation theory.
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.
authors.affiliation: Chemistry Department, Imam Khomeini International University, Qazvin, Iran. grb402003@yahoo.com
authors.forename: G Rezaei
authors.initials: GR
authors.lastname: Behbehani
authors.forename: A A
authors.initials: AA
authors.lastname: Saboury
authors.forename: A
authors.initials: A
authors.lastname: Divsalar
mesh_terms: D000818:Animals; D002118:Calcium / Q000378:metabolism*; D002412:Cations; D002417:Cattle; D008274:Magnesium / Q000378:metabolism*; D008962:Models, Theoretical; D004676:Myelin Basic Protein / Q000378:metabolism*; D012995:Solubility; D013816:Thermodynamics
chemical_list: D002412:Cations; D004676:Myelin Basic Protein; D008274:Magnesium; D002118:Calcium