Globular proteins exhibit dielectrophoresis (DEP) responses in experiments where the applied field gradient factor backward difference E-2 appears far too small, according to standard DEP theory, to overcome dispersive forces associated with the thermal energy kT of disorder. To address this a DEP force equation is proposed that replaces a previous empirical relationship between the macroscopic and microscopic forms of the Clausius-Mossotti factor. This equation relates the DEP response of a protein directly to the dielectric increment delta epsilon(+) and decrement delta epsilon(-) that characterize its beta-dispersion at radio frequencies, and also indirectly to its intrinsic dipole moment by way of providing a measure of the protein's effective volume. A parameter Gamma(pw), taken as a measure of cross-correlated dipole interactions between the protein and its water molecules of hydration, is included in this equation. For 9 of the 12 proteins, for which an evaluation can presently be made, Gamma(pw) has a value of approximate to 4600 +/- 120. These conclusions follow an analysis of the failure of macroscopic dielectric mixture (effective medium) theories to predict the dielectric properties of solvated proteins. The implication of a polarizability greatly exceeding the intrinsic value for a protein might reflect the formation of relaxor ferroelectric nanodomains in its hydration shell.