NDLI: Binding properties and structural changes of human growth hormone upon interaction with cobalt ion

Content Provider	Springer Nature Link
Author	Saboury, A. A. Ghourchaei, H. Sanati, M. H. Atri, M. S. Rezaei Tawirani, M. Hakimelahi, G. H.
Copyright Year	2007
Abstract	Binding properties and structural changes of human growth hormone (hGH) due to the interaction by cobalt ion (Co$^{2+}$) were done at 27°C in NaCl solution, 50 mM, using different techniques of UV-Vis spectroscopy, circular dichroism (CD), isothermal titration calorimetry (ITC) and differential scanning calorimetry (DSC) techniques. There is a set of three identical and non-interacting binding sites for cobalt ions. The intrinsic association equilibrium constant and the molar enthalpy of binding obtained by ITC are 0.80 mM$^{−1}$ and −16.70 kJ mol$^{−1}$, respectively. The intrinsic association equilibrium constant obtained by a standard isothermal titration UV-Vis spectrophotometry method is also 0.79 mM$^{−1}$, which is in good agreement with the value obtained from ITC. The Gibbs free energy and entropy changes due to the binding of cobalt ion on hGH are −16.67 kJ mol$^{−1}$ and −0.1 J K$^{−1}$ mol$^{−1}$, respectively. Energetic domains analysis by DSC shows that phase transition of hGH in the presence of cobalt occurs at one main transition. Deconvolution of the main transition provides two sub-transitions with different values of the melting point and enthalpy of unfolding (33°C and 164 kJ mol$^{−1}$ for the first and 49°C and 177 kJ mol$^{−1}$ for the second, respectively). Interaction of cobalt ions with hGH prevents aggregation by an affect on the hydrophobicity of the protein macromolecule and provide useful information about its structure due to becoming reversible of protein thermal denaturation.
Starting Page	921
Ending Page	927
Page Count	7
File Format	PDF
ISSN	13886150
Journal	Journal of thermal analysis
Volume Number	89
Issue Number	3
e-ISSN	15728943
Language	English
Publisher	Springer US
Publisher Date	2006-10-20
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	circular dichroism cobalt human growth hormone protein stability titration calorimetry Measurement Science, Instrumentation Inorganic Chemistry Physical Chemistry Polymer Sciences
Content Type	Text
Resource Type	Article
Subject	Physical and Theoretical Chemistry Condensed Matter Physics

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