1. A set of parameters is proposed to check the interpretation of the dielectric behaviour of protein solutions as a rigid-dipole relaxation of prolate ellipsoids of revolution in the frequency range between 20 kHz and 10 MHz. Besides the δb-function of Scheraga, another analogous function (δa) is presented to establish size and shape of globular proteins. A study of the influence of solvent viscosity on the dielectric dispersion also gives strong evidence in favour of rigid-dipole relaxation. 2. Measurements of the dielectric dispersion of monomer solutions of bovine serum albumin and transferrin are reported. Monomers of bovine serum albumin were obtained by fractionation on Sephadex G-150. Low-conductivity solutions of both proteins are obtained by passage through an ion-exchange resin. 3. Computer analysis of the experimental dispersion curves by use of a two-term Debye dispersion gives valuable information about transferrin and leads to an axial ratio 4·5 for a prolate ellipsoid of revolution. The dielectric increment of bovine serum albumin is very low and no conclusive results have yet been obtained.
Research Article| December 01 1968
The dipolar origin of protein relaxation
M. Y. Rosseneu-Motreff;
Biochem J (1968) 110 (3): 419–424.
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H. Hendrickx, R. Verbruggen, M. Y. Rosseneu-Motreff, V. Blaton, H. Peeters; The dipolar origin of protein relaxation. Biochem J 1 December 1968; 110 (3): 419–424. doi: https://doi.org/10.1042/bj1100419
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