D-RIBOSE STABILIZES PRECURSOR AND MATURE RIBOSE-BINDING PROTEINS OF ESCHERICHIA-COLI

Abstract

Heat- and guanidine hydrochloride-induced unfolding and refolding of precursor as well as mature ribose-binding proteins of Escherichia coli were studied in the presence of D-ribose using intrinsic tyrosine fluorescence and circular dichroism. The precursor and mature proteins have shown virtually identical unfolding-folding behavior. It was observed that D-ribose refolds partially unfolded precursor and mature ribose binding proteins into native structure and decreases the unfolding rate of the these proteins. The conformational stabilities of these proteins were found to increase with increasing D-ribose concentration.