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   <subfield code="a">Thermodynamic Study of the Binding of Mercury Ion to Human Growth Hormone at Different Temperatures</subfield>
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   <subfield code="c">[E. Lemeski, G. Behbehani, A. Saboury, M. Monajjemi, R. Mehrabian, M. Golsefidi, H. Rajabzadeh, M. Baei, S. Hasanzadeh]</subfield>
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   <subfield code="a">The interaction of human growth hormone (hGH) with the divalent mercury ion was studied by isothermal titration calorimetry at two temperatures of 27 °C and 37 °C in aqueous solutions. We found that there is a set of two identical and non-interacting binding sites for Hg2+ ions. The intrinsic dissociation equilibrium constant and the molar enthalpy of binding are 4.2 mmol⋅L−1 and −14.8 kJ⋅mol−1 at 27 °C and 5.1 mmol⋅L−1 and −14.2kJ⋅mol−1 at 37 °C, respectively. The results obtained indicate that the stability of the protein increases due to the binding of mercury ions using the extended solvation theory.</subfield>
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