A thermodynamic study on the binding of magnesium with human growth hormone - Consideration of the new extended coordination model solvation parameters
A thermodynamic study on the binding of magnesium with human growth hormone - Consideration of the new extended coordination model solvation parameters
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DOI:
10.1007/s10973-006-8206-x
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发表时间:
2007-09-01
影响因子:
4.4
通讯作者:
Saboury, A. A.
中科院分区:
文献类型:
--
作者:
Behbehani, G. Rezaei;Saboury, A. A.
The thermodynamic parameters underlying the binding of Mg2+ to the hydrophobic core of human growth hormone, hGH, are determined using isothermal titration calorimetry. The interaction between Mg2+ and hGH (35 mu M) was studied at 27 degrees C in NaCl solution. A new solvation model was used to reproduce the enthalpies of Mg2+-hGH interaction over the whole Mg2+ concentrations. The solvation parameters recovered from the new salvation model, were correlated to the structural changes of hGH due to the metal ion interaction.