Thermodynamic study of the binding of calcium and magnesium ions with myelin basic protein using the extended solvation theory

• 来源期刊: 生物化学与生物物理学报（英文版）
• 关键词: myelin basic protein isothermal titration calorimetry binding parameter
• 年，卷（期）: 2008,（11）
• 页码范围: 964-969
• 页数: 6页
• 语种: 英文
• DOI: 10.1111/j.1745-7270.2008.00477.x

摘要

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℃ in aqueous solution. The extended solvation model was used to reproduce the enthaipies 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.