Osmolyte Effect on Denaturation on Proteins

Abstract

Plants, animals, and microorganisms have adapted to such environmental stress by evolving means to protect their proteins and other cell components against such denaturing stress. Denaturants, such as urea and guanidinium chloride (GdmCl), destabilize proteins. In contrast, osmolytes that protect cells against environmental stresses such as high temperature, desiccation, and pressure can stabilize proteins. Thus, a complete understanding of the stability of proteins and a description of the structures in the diverse DSEs requires experimental and theoretical studies that provide a quantitative description of the effects of both osmolytes and denaturants. The diffusion constant does not show any change in presence of increasing concentration of BSA. It is also found from the experiment that the number of bound urea molecule to the GlnRS surface reduced markedly in the presence of 0.25 M TMAO as osmolytes. So it may be concluded that preferential exclusion, due to steric repulsion is best fitted to explain the protective action of osmolytes. Osmolytes leads to the compactation of the protein molecule, due to the steric repulsion eventually ending up with expulsion of urea from the protein core