Thermodynamic Study of Myelin Basic Protein upon Interaction with [Hg²⁺] Using Extension Solvation Model

Abstract

Mercury ion interaction with myelin basic protein (MBP) was studied at 300 K in 30 mmol/L tris buffer, pH＝7 by isothermal titration calorimetry (ITC). An extended solvation model was used for Hg 2＋ ＋MBP interaction over the whole range of Hg 2＋ concentrations. The binding parameters recovered from the solvation model were attributed to the structural changes of MBP due to its interaction with mercury ion. It was found that mercury ion acted as a noncooperative effector of MBP, and there is a set of two identical and independent binding sites for Hg 2＋ ions.The dissociation equilibrium constant is 97.6 µmol/L. The molar enthalpy change of binding is -11.25 kJ•mol -1 .

Applications of isothermal titration calorimetry in pure and applied research—survey of the literature from 2010

“…Protein interactions with small ligands (including co‐factors and drugs) Protein/peptide interactions with metals and ions Protein/peptide interactions with nucleic acids …”

A Comparative Study on the Interaction of Sulfonamide and Nanosulfonamide with Human Serum Albumin

“…For a set of identical and independent binding sites, a plot of (Δ max ) [ / , through which and can be obtained [15][16][17][18][19] as follows:…”