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Thermodynamic study of the binding of calcium and magnesium ions with myelin basic protein using the extended solvation theory
Article first published online: 1 DEC 2008
DOI: 10.1111/j.1745-7270.2008.00477.x
© 2008 Institute of Biochemistry and Cell Biology, SIBS, CAS
Additional Information
How to Cite
Behbehani, G. R., Saboury, A. A. and Divsalar, A. (2008), Thermodynamic study of the binding of calcium and magnesium ions with myelin basic protein using the extended solvation theory. Acta Biochimica et Biophysica Sinica, 40: 964–969. doi: 10.1111/j.1745-7270.2008.00477.x
Publication History
- Issue published online: 1 DEC 2008
- Article first published online: 1 DEC 2008
- Received: August 25, 2008 Accepted: September 29, 2008
- Abstract
- References
- Cited By
Keywords:
- myelin basic protein;
- isothermal titration calorimetry;
- binding parameter
The interaction of myelin basic protein (MBP) from the bovi ne central nervous system with Ca2+ and Mg2+ ions, named as M2+, was studied by isothermal titration calorimetry at 27 °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.