The dielectric estimation of protein hydration

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Abstract
Microwave dielectric measurements on six aqueous protein solutions are analyzed in terms of water 'irrotationally bound' to the protein, i.e. unable to rotate in the high-frequency field. Estimates are made of the maximum amount of bound water, i.e. water carried through the solution with the protein, as a function of axial ratio, assuming a spheroid molecule. Taking hydration estimates in conjunction with other data, we conclude inter alia: (1) That the $\beta $-lactoglobulin and egg-albumin molecules approximate to prolate rather than to oblate spheroids. (2) That a large proportion of the charged groups in horse methaemoglobin 'protrude' from the surface of the molecule.

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