Abstract
The preferential interaction of the solvent components with β-lactoglobulin and chymotrypsinogen A, respectively, was determined in aqueous urea solutions by means of equilibrium dialysis and differential refractometry. It has been found that at all concentration studied urea was preferentially bound. Using a modified equilibrium dialysis technique the total urea binding to the two proteins was also obtained. Total urea binding increases with increasing urea concentration. In 8 M urea where the two proteins are completely unfolded there is about one urea molecule per three amino acid residues. The results obtained strongly suggest that the extent of urea interaction with protein is the decisive factor in bringing about the unfolding of protein molecules.
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