Characterization of Stress Responsive Behaviors of Proteins

Abstract

Protein denaturation processes under stress conditions such as pH, denaturant and heat are evaluated by employing several approaches such as aqueous two-phase partitioning and circular dichroism (CD) measurement in order to determine the conformational states and surface properties of proteins. It is suggested that the manner of conformational change of protein from the native state to the molten globule one does not depend on these sorts of stresses if both the strength of stress and surface properties of proteins are normalized between the above two states. By using these normalization parameters, eight proteins used in this study were simply divided into two groups namely monomeric proteins and oligomeric one. On the other hand, the strength of stress which inducing protein denaturation up to the molten globule state greatly depends on the sort of stresses or protein species. From these considerations, the possibility of using effective stress-mediated separation process of protein is suggested as an application of the analysis of the stress responsive behaviors of proteins.