Document Type: Research Article
Institute of Biochemistry & Biophysics University of Tehran, P.O. Box 13145-1384 Tehran, I.R. IRAN
A Study was made on the interaction between histon H1 and sodium n-dodecyl sulphate (SDS) in the presence of sodium arsenate inside a phosphate buffer of pH 6.4, using spectroscopy and equilibrium dialysis at 27 °C. The binding data has been used to obtain the gibbs free energy in terms of a theoretical model based on the Wyman binding potential. The binding data hs been analysed in terms of Hill equation, to obtain Hill coefficient. The data show that sodium arsenate exhibits an unusually greater degree of denaturation for the structure of H1.