The Experts below are selected from a list of 258960 Experts worldwide ranked by ideXlab platform
Kamahldin Haghbeen - One of the best experts on this subject based on the ideXlab platform.
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effects of calcium binding on the structure and stability of human growth hormone
International Journal of Biological Macromolecules, 2005Co-Authors: Ali Akbar Saboury, Maliheh Sadat Atri, Mohammad Hossein Sanati, A A Moosavimovahedi, Kamahldin HaghbeenAbstract:Abstract Thermodynamic analysis of calcium ions binding to human growth hormone (hGH) was done at 27 °C in NaCl solution, 50 mM, using different techniques. The binding isotherm for hGH-Ca 2+ was obtained by two techniques of ionmetry, using a Ca 2+ -selective membrane electrode, and isothermal titration calorimetry. Results obtained by two ionmetric and calorimetric methods are in good agreement. There is a set of three identical and non-interacting binding sites for calcium ions. The intrinsic dissociation equilibrium constant and the molar enthalpy of binding are 52 μM and −17.4 kJ/mol, respectively. Temperature scanning UV–vis spectroscopy was applied to elucidate the effect of Ca 2+ binding on the protein stability, and circular dichroism (CD) spectroscopy was used to show the structural change of hGH due to the metal ion Interaction. Calcium ions binding increase the protein thermal stability by increasing of the alpha helix content as well as decreasing of both beta and random coil structures.
Ali Akbar Saboury - One of the best experts on this subject based on the ideXlab platform.
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using the extended solvation theory for thermodynamic study on the Interaction of magnesium and cobalt ions with human growth hormone
Journal of The Korean Chemical Society, 2008Co-Authors: Rezaei G Behbehani, Ali Akbar Saboury, Adeleh DivsalarAbstract:A thermodynamic study on the Interaction between magnesium and cobalt ions (M), and human growth hormone, hGH, was studied at 27 °C in NaCl solution (50 mM) using the isothermal titration calorimetry. Isothermal titration calorimetry was applied to obtain the binding isotherm for hGH+M. The results obtained indicate that there is a set of three identical and noninteracting binding sites for Cobalt ions and a set of two for magnesium. The extended solvation model was used to reproduce the enthalpies of M+hGH Interactions over the whole metal ions concentrations. The solvation parameters recovered from the solvation model were attributed to the structural change of hGH due to the metal ion Interaction. The extended solvation model was applied to elucidate the effect of Mg and Co binding on the protein stability.
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a thermodynamic study on the binding of calcium ion with myelin basic protein
Journal of Solution Chemistry, 2007Co-Authors: Rezaei G Behbehani, Ali Akbar Saboury, Fallah A BagheryAbstract:The Interaction of myelin basic protein (MBP) from the bovine central nervous system with divalent calcium ion was studied by isothermal titration calorimetry at 27 °C in aqueous solution. The extended solvation model was used to reproduce the enthalpies of Ca2+-MBP Interaction over the whole range of Ca2+ concentrations. The solvation parameters recovered from the 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 non-interacting binding sites for Ca2+ ions. The association equilibrium constant is 0.021 μmol⋅dm−3. The molar enthalpy of binding is ΔH=−15.10 kJ⋅mol−1.
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effects of calcium binding on the structure and stability of human growth hormone
International Journal of Biological Macromolecules, 2005Co-Authors: Ali Akbar Saboury, Maliheh Sadat Atri, Mohammad Hossein Sanati, A A Moosavimovahedi, Kamahldin HaghbeenAbstract:Abstract Thermodynamic analysis of calcium ions binding to human growth hormone (hGH) was done at 27 °C in NaCl solution, 50 mM, using different techniques. The binding isotherm for hGH-Ca 2+ was obtained by two techniques of ionmetry, using a Ca 2+ -selective membrane electrode, and isothermal titration calorimetry. Results obtained by two ionmetric and calorimetric methods are in good agreement. There is a set of three identical and non-interacting binding sites for calcium ions. The intrinsic dissociation equilibrium constant and the molar enthalpy of binding are 52 μM and −17.4 kJ/mol, respectively. Temperature scanning UV–vis spectroscopy was applied to elucidate the effect of Ca 2+ binding on the protein stability, and circular dichroism (CD) spectroscopy was used to show the structural change of hGH due to the metal ion Interaction. Calcium ions binding increase the protein thermal stability by increasing of the alpha helix content as well as decreasing of both beta and random coil structures.
A A Moosavimovahedi - One of the best experts on this subject based on the ideXlab platform.
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effects of calcium binding on the structure and stability of human growth hormone
International Journal of Biological Macromolecules, 2005Co-Authors: Ali Akbar Saboury, Maliheh Sadat Atri, Mohammad Hossein Sanati, A A Moosavimovahedi, Kamahldin HaghbeenAbstract:Abstract Thermodynamic analysis of calcium ions binding to human growth hormone (hGH) was done at 27 °C in NaCl solution, 50 mM, using different techniques. The binding isotherm for hGH-Ca 2+ was obtained by two techniques of ionmetry, using a Ca 2+ -selective membrane electrode, and isothermal titration calorimetry. Results obtained by two ionmetric and calorimetric methods are in good agreement. There is a set of three identical and non-interacting binding sites for calcium ions. The intrinsic dissociation equilibrium constant and the molar enthalpy of binding are 52 μM and −17.4 kJ/mol, respectively. Temperature scanning UV–vis spectroscopy was applied to elucidate the effect of Ca 2+ binding on the protein stability, and circular dichroism (CD) spectroscopy was used to show the structural change of hGH due to the metal ion Interaction. Calcium ions binding increase the protein thermal stability by increasing of the alpha helix content as well as decreasing of both beta and random coil structures.
Mohammad Hossein Sanati - One of the best experts on this subject based on the ideXlab platform.
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effects of calcium binding on the structure and stability of human growth hormone
International Journal of Biological Macromolecules, 2005Co-Authors: Ali Akbar Saboury, Maliheh Sadat Atri, Mohammad Hossein Sanati, A A Moosavimovahedi, Kamahldin HaghbeenAbstract:Abstract Thermodynamic analysis of calcium ions binding to human growth hormone (hGH) was done at 27 °C in NaCl solution, 50 mM, using different techniques. The binding isotherm for hGH-Ca 2+ was obtained by two techniques of ionmetry, using a Ca 2+ -selective membrane electrode, and isothermal titration calorimetry. Results obtained by two ionmetric and calorimetric methods are in good agreement. There is a set of three identical and non-interacting binding sites for calcium ions. The intrinsic dissociation equilibrium constant and the molar enthalpy of binding are 52 μM and −17.4 kJ/mol, respectively. Temperature scanning UV–vis spectroscopy was applied to elucidate the effect of Ca 2+ binding on the protein stability, and circular dichroism (CD) spectroscopy was used to show the structural change of hGH due to the metal ion Interaction. Calcium ions binding increase the protein thermal stability by increasing of the alpha helix content as well as decreasing of both beta and random coil structures.
Maliheh Sadat Atri - One of the best experts on this subject based on the ideXlab platform.
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effects of calcium binding on the structure and stability of human growth hormone
International Journal of Biological Macromolecules, 2005Co-Authors: Ali Akbar Saboury, Maliheh Sadat Atri, Mohammad Hossein Sanati, A A Moosavimovahedi, Kamahldin HaghbeenAbstract:Abstract Thermodynamic analysis of calcium ions binding to human growth hormone (hGH) was done at 27 °C in NaCl solution, 50 mM, using different techniques. The binding isotherm for hGH-Ca 2+ was obtained by two techniques of ionmetry, using a Ca 2+ -selective membrane electrode, and isothermal titration calorimetry. Results obtained by two ionmetric and calorimetric methods are in good agreement. There is a set of three identical and non-interacting binding sites for calcium ions. The intrinsic dissociation equilibrium constant and the molar enthalpy of binding are 52 μM and −17.4 kJ/mol, respectively. Temperature scanning UV–vis spectroscopy was applied to elucidate the effect of Ca 2+ binding on the protein stability, and circular dichroism (CD) spectroscopy was used to show the structural change of hGH due to the metal ion Interaction. Calcium ions binding increase the protein thermal stability by increasing of the alpha helix content as well as decreasing of both beta and random coil structures.