پديدآورندگان :
Saboury A. Department of BioChemistry and Biophysics, University of Tehran, Tehran, Iran , Rezaei Behbehani G. Department of Chemistry , Faculty of science, University of Ghazvin, Ghazvin, Iran , Ramzani S. mojgan_905@yahoo.com Department of Chemistry , Faculty of science, University of Ghazvin, Ghazvin, Iran;
چكيده فارسي :
The interaction of Sodium Dodecyl Sulfate (SDS) with hen egg lysozyme have been investigated in 298, 303 and 308 K in phosphate buffer at two different pH values (5 and 7), by isothermal titration calorimetry. The negative SDS ion binds to positive residues, neutralizes the protein surface charges and leads to precipitation and turbidity of the solution. At low concentrations of SDS, the binding is mainly electrostatic, with some simultaneous interaction of the hydrophobic tail with nearby hydrophobic patches on the lysozyme.
