in the present study, the binding isotherms for interaction of a homologous series of n-alkyltrimethyl ammonium bromides with bovine serum albumin (bsa) have been analyzed on basis of intrinsic thermodynamic quantities. in this regards, the intrinsic gibbs free energy of binding, agb(i,)„ has been estimated at various surfactant concentrations and its trend of variation for both binding sets ha...

The binding data for interaction of a homologous series of n-alkyl sulfates with alkyl chainlengths from C8 to C12 with insulin were analyzed on basis of Hill equation for two classes ofbinding sites .The intrinsic Gibbs free energies were calculated and resolute on basis ofelectrostatic and hydrophobic contributions The estimation of these contributions reveals themajor role of electrostatic i...