[Globular protein hydration by a differential dielectrometric method]

A differential method is described for measuring dielectric constants and losses in aqueous protein solutions at millimetrerange wavelengths. Employment of the method allows to improve the accuracy of determining the degree of hydratation. A method has also been suggested for taking into account the contribution of ions to the dielectric constant of solutions. The differential method was used to study hydratation of nine globular proteins. The data obtained are compared with the corresponding values provided by other experimental techniques and with theoretical predictions based on some models of hydratation. Good agreement is obtained with results provided by the isopiestic and NMR techniques. The discrepancy shown for hemoglobin is discussed in the paper. As has been shown, the dielectric method registers a monomolecular surface layer of water only. With pH varying between 4.0 and 3.2, a significant increase is observed in the hydratation of serum albumin. Presumably, this effect is connected with a N--F conformational transition.