INTERACTION STUDIES BETWEEN IONS AND PROTEINS AT PHYSIOLOGICALLY RELEVANT CONCENTRATIONS

Abstract

Currently, protein-ion interactions are commonly believed to be dominated by nonspecific electrostatic screening effects. In our study, by using NMR HSQC titrations, we studied the effects of different salts on both unstructured and well-folded proteins in water, thus eliminating the intrusion of background buffers. We found that in contrast to the common belief, different anions could bind to proteins at distinctive residues with high specificities and affinities for both the unstructured and the well folded protein. So we speculate that such bindings would also occur to other proteins. Consequently, without a deep understanding of anion-protein interactions, we will fail to comprehend how proteins function in cells.