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dc.contributor.authorErmolina, I.en
dc.contributor.authorFedotov,V.en
dc.contributor.authorFeldman, Yurien
dc.contributor.authorIvoylov, I.en
dc.date.accessioned2017-11-22T09:35:49Z
dc.date.available2017-11-22T09:35:49Z
dc.date.issued1994-09-01
dc.identifier.citationErmolina et al. (1994) Investigation of molecular motion and interprotein interactions in solutions by TDDS: A comparison with NMR data. Journal of Non-Crystalline Solids, 172-174 (2), pp. 1103-1108.en
dc.identifier.urihttp://hdl.handle.net/2086/14892
dc.description.abstractThe 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 otational 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.en
dc.publisherElsevieren
dc.subjectProtein molecular motionen
dc.subjectdieletric spectroscopyen
dc.subjectNMRen
dc.titleInvestigation of molecular motion and interprotein interactions in solutions by TDDS: A comparison with NMR dataen
dc.typeArticleen
dc.identifier.doihttps://doi.org/10.1016/0022-3093(94)90629-7
dc.peerreviewedYesen
dc.funderN/Aen
dc.projectidN/Aen
dc.cclicenceCC-BY-NCen
dc.researchinstituteLeicester Institute for Pharmaceutical Innovation - From Molecules to Practice (LIPI)en


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