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. 1968 Dec;110(3):419–424. doi: 10.1042/bj1100419

The dipolar origin of protein relaxation

H Hendrickx 1, R Verbruggen 1, M Y Rosseneu-Motreff 1, V Blaton 1, H Peeters 1
PMCID: PMC1187367  PMID: 5701669

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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