Dielectric relaxation, molecular motion and interprotein interactions in myoglobin solution.

Date

1997

Advisors

Journal Title

Journal ISSN

ISSN

Volume Title

Publisher

Taylor and Francis

Type

Article

Peer reviewed

Yes

Abstract

The results of the investigation of protein molecule dynamic in solution by Time Domain Dielectric Spectroscopy are presented. The horse myoglobin solutions in wide range of concentration from 0.6% to 54% at 20°C have been investigated. The result of analysis produced in the term of dipole correlation function has shown that the obtained correlation function of macromolecule motion may be presented as sum of three components corresponding to three kinds of protein motions: anisotropic intramolecular motion, anisotropic Brownian tumbling and isotropic slow motion. We suppose that the cause of protein tumbling anisotropy and the possibility to keep slow motion is the interprotein electrostatic interactions. The characteristic time of slow motion depends on the concentration of protein and perhaps is controlled by translational diffusion. The dipole moment of myoglobin calculated by the Onsager-Oncley equation is 200D for solutions less than 10% protein concentration. It is in a good agreement with the theoretical value.

Description

Keywords

protein molecule dynamics, horse myoglobin, intramolecular motion, Brownian tumbling, slow motion

Citation

Ermolina, I. et al. (1997) Dielectric relaxation, molecular motion and interprotein interactions in myoglobin solution. Journal of Biomolecular Structure and Dynamics,15 (2), pp.381-392.

Rights

Research Institute

Leicester Institute for Pharmaceutical Innovation - From Molecules to Practice (LIPI)