Open AccessThermodynamic study of the binding of calcium and magnesium ions with myelin basic protein using the extended solvation theory
Author(s) -
Behbehani G. Rezaei,
Saboury A. A.,
Divsalar A.
Publication year - 2008
Publication title -
acta biochimica et biophysica sinica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.771
H-Index - 57
eISSN - 1745-7270
pISSN - 1672-9145
DOI - 10.1111/j.1745-7270.2008.00477.x
Subject(s) - solvation , isothermal titration calorimetry , chemistry , myelin basic protein , magnesium , solvation shell , ion , metal ions in aqueous solution , implicit solvation , aqueous solution , titration , crystallography , inorganic chemistry , computational chemistry , myelin , central nervous system , organic chemistry , biology , neuroscience
The interaction of myelin basic protein (MBP) from the bovi ne central nervous system with Ca 2+ and Mg 2+ ions, named as M 2+ , was studied by isothermal titration calorimetry at 27 °C in aqueous solution. The extended solvation model was used to reproduce the enthalpies of MBP+M 2+ 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 Ca 2+ and Mg 2+ ions.