Investigation of molecular motion and interprotein interactions in solutions by TDDS: a comparison with NMR data

Irina Ermolina, Vladimir Fedotov, Yuri Feldman*, Igor Ivoylov

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

Abstract

The results of dynamic protein behavior in solution studied by time domain dielectric spectroscopy (TDDS) are presented. The analyses for myoglobin solutions at concentrations 50, 120 and 150 mg/ml in the temperature interval from 5 to 35°C was carried out in terms of dipole correlation functions. It was found that the correlation function of the protein motion can be presented as a sum of three components corresponding to three types of protein motion: internal local motion, anisotropy rotational Brownian diffusion and translational Brownian diffusion. According to the hypothesis presented earlier, it is supposed that the reason for anisotropy of protein rotation and capability for the detection translational diffusion (slowest motion) is the mutual interprotein electrostatic steering.

Original languageEnglish
Pages (from-to)1103-1108
Number of pages6
JournalJournal of Non-Crystalline Solids
Volume172-174
Issue numberPART 2
DOIs
StatePublished - 1 Sep 1994

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