The permittivities of three solutions of sperm-whale myoglobin of different concentrations were measured in the frequency range 300-1300MHz at 20 degrees C by using a coaxial-line technique. These results were combined with those measured previously at frequencies below 10MHz. Two methods are described for calculating the extent of macromolecular hydration from the data. The more reliable method yields results of approx. 0.25g of H(2)O/g of protein, which is in satisfactory agreement with the theoretically calculated value. Agreement with the value found from the rotational motion of the molecule is not so close, which is probably caused by the different meanings that may be ascribed to the term hydration.

The relative permittivity and conductivity of aqueous solutions of oxyhaemoglobin and carboxyhaemoglobin were measured over the frequency range 150kHz-100MHz. To minimize errors of measurement the investigations were carried out with three different samples of each type of haemoglobin, independent apparatus being used in two different laboratories. The dielectric increment and relaxation time were calculated at each of several temperatures from the results. These lead to a dipole moment of 400 Debyes and an activation enthalpy of 17.6+/-1.4kJ.mol(-1), both of which were found to be independent of temperature to within experimental error over the range 3-35 degrees C. The value of the dipole moment shows that the distribution of charge throughout the haemoglobin molecule is nearly symmetrical with respect to the centre of charge. The magnitude of the activation enthalpy is similar to that of the viscosity of water, in accord with the common observation that dielectric relaxation and viscosity are related phenomena. No significant differences are found between the dielectric parameters of oxyhaemoglobin and carboxyhaemoglobin. Combining the results with those obtained from X-ray diffraction of the solid a hydration value of 0.45g of water/g of protein is suggested, subject to the limitations of the model used. Finally, the results indicate the presence of a subsidiary dispersion, which could be attributed to the above quantity of bound water having a static permittivity of about 100 and a relaxation frequency in the region 100-200MHz.

The parameters of dielectric dispersion at radio frequencies in aqueous solutions of horse and sperm whale myoglobin have been measured as functions of protein concentration, solution conductivity and temperature. From these dependences it is shown that, of the likely interpretations, the mechanism of molecular rotation is best able to account for the observed dispersion. The results are consistent with a dipole moment of around 150D for the myoglobin molecule and a hydration shell of about two water molecules thickness. This value of dipole moment is shown to be in good agreement with that obtained from calculations based on the known crystal structure.

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The problem of the absorption of the energy of plane electromagnetic radiation by an aqueous solution of macromolecules is considered. A simplified model for the hydrated molecule is employed, consisting of a spherical shell of bound water surrounding a spherical core. The power deposition per unit volume of the shell is calculated in the frequency range 100 MHz-100 GHz for several bound water relaxation frequencies. In each case the corresponding values are also calculated for free water for comparison. The values obtained for the bound water are shown to be significantly higher than those for the free water up to frequencies of at least 1 GHz. The maximum difference between these two sets of values is of the order of a factor of five and occurs roughly at the bound water relaxation frequency. Because of the strong coupling between the bound water molecules and the macromolecules present in biological material this result could be a significant factor in the explanation of the biological effects of microwaves at a molecular level.