The binding of Sodium n-dodecyl sulphate (SDS) to histone H3 was studied in the pH range 3.2-10 by equilibrium dialysis at 27? and 3 7 ?c .T he binding data have been used to obtain the Gibbs free energy of interaction using a theoretical model of the Wyman binding potential; and the enthalpy of interaction from the temperature dependence of theequilibriumconstantsfronr theVan't Hoff re1ati...

A thermodynamic study of copper ions by jack bean urease (JBU) was carried out at two temperatures of 27 and 37?C in Tris buffer (30 mM; pH=7.0) using an isothermal titration calorimetry. There is a set of twelve identical and non-interacting binding sites for copper ions. The intrinsic dissociation equilibrium constant and the molar enthalpy of binding are 285 µM and ?15.2 kJ/mol at 27?C and 3...

The interaction between isatin-β-thiosemicarbazone (IBT) and calf thymus DNA (CT-DNA) was investigated in physiological buffer (pH 7.4) using Neutral Red (NR) dye as a spectral probe by UV–Vis absorption and fluorescence spectroscopy, as well as viscosity measurements. The IBT is stabilized by intercalation in the DNA ( K [IBT –DNA] =1.03×105 M−1), and displaces the NR dye from the NR–DNA comple...

The interaction between isatin-β-thiosemicarbazone (IBT) and calf thymus DNA (CT-DNA) was investigated in physiological buffer (pH 7.4) using Neutral Red (NR) dye as a spectral probe by UV–Vis absorption and fluorescence spectroscopy, as well as viscosity measurements. The IBT is stabilized by intercalation in the DNA ( K [IBT –DNA] =1.03×105 M−1), and displaces the NR dye from the NR–DNA comple...

the interaction of hgh with some metal ions ( ) at 27°c in nac1 solution, 50 mm was studied using isothermal titration calorimetry. there is a set of three identical and non-interacting binding sites for binding of all these metal ions, expect . the intrinsic association equilibrium constants () are not very different for  and , and also their molar enthalpies of binding (kj/mol for  and  kj/mo...

a binding study of nickel ions by a new recombinant human growth hormone (hgh), produced as an injected drug, has been done at 27˚c in nacl solution (50 mm) using an isothermal titration calorimetry. there is a set of three identical and non-interacting binding sites for nickel ions. the intrinsic dissociation equilibrium constant and the molar enthalpy of binding are 40 μm and -16.5 kj/mol, re...

The interaction of histone H2B and dodecyl trimethyl ammonium bromide (DTAB) was studies via equilibrium dialysis method at two different temperatures, at pH 6.4 in phosphate buffer. The binding data were used to obtain the Gibbs free energy of interaction, which is interpreted in terms of a theoretical model based on the Wyman binding potential. The data were then used to obtain...

The interaction of hGH with some metal ions ( ) at 27°C in NaC1 solution, 50 mM was studied using Isothermal titration calorimetry. There is a set of three identical and non-interacting binding sites for binding of all these metal ions, expect . The intrinsic association equilibrium constants () are not very different for  and , and also their molar enthalpies of binding (KJ/mol for  and  KJ/mo...

A binding study of nickel ions by a new recombinant human Growth Hormone (hGH), produced as an injected drug, has been done at 27˚C in NaCl solution (50 mM) using an isothermal titration calorimetry. There is a set of three identical and non-interacting binding sites for nickel ions. The intrinsic dissociation equilibrium constant and the molar enthalpy of binding are 40 μM and -16...

This paper is designed to examine the binding behavior of Coumarin with bovine -casein (βCN) through fluorescence spectroscopy and molecular modeling techniques. The data analysis on fluorescence titration experiments at various temperatures represents the enthalpy driven nature for the formation of Coumarin–βCN complex and the prevailed role of hydrogen bonds and van der Waals interactions in...