Studies on Solvation Behavior of Some Amino Acids and Lysozyme in Mixed Aqueous Solutions of
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چکیده
The native state of protein is a resultant of delicate balance of various interactions of protein within itself and with surrounding environment. Disruption of this balance by heat, cold, pressure, pH, denaturant etc., leads to protein denaturation. In the present paper we have investigated the effect of sodium acetate, magnesium acetate calcium acetate, sodium propionate and sodium butyrate on thermal stability and preferential solvation changes accompanying the thermal unfolding of lysozyme at pH = 1.5 by UV-Visible Spectrophotometer. The two state (N↔D) reversible transition was observed for these systems. Thermal denaturation in these systems is explained on the basis of competing patterns of interactions of the cosolutes with native vs. denatured states of protein. It has been observed that sodium acetate, magnesium acetate and calcium acetate stabilize while sodium propionate and sodium butyrate destabilize the lysozyme. The order of stabilization by cations i.e. Na > Mg > Ca and by anions i.e. acetate > propionate > butyrate observed presently also follows the Hofmeister series. The preferential interaction parameters from these thermodynamic data and by correlating the surface tension of these cosolutes with surface area of lysoyzme have also been calculated.
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تاریخ انتشار 2006