Browsing by Author "Fedotov, V."

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    Investigation of molecular motions and interprotein interactions in solutions by NMR and TDDS.
    (Springer, 1993) Ermolina, I.; Krushelnitsky, A. G.; Ivoylov, I.; Feldman, Yuri; Fedotov, V.
    Non-selective NMR relaxation of protein and water protons at various resonance frequencies as well as Time Domain Dielectric Spectroscopy (TDDS) were applied to study the molecular motions in lysozyme and myoglobin solutions. It was found that the correlation function of the protein motion defined by means of all these methods can be presented as a sum of three components having substantially different correlation times. Both NMR and TDDS experimental data were treated on the basis of approach according to which these components of the correlation function correspond to three different kinds of protein motion, namely 1) internal local motion, 2) anisotropic rotational Brownian diffusion and 3) translational Brownian diffusion. According to the hypothesis proposed earlier we suppose that the reason of anisotropy of protein rotation and possibility to detect experimentally the slowest motion (translational diffusion) is the mutual interprotein electrostatic steering. The qualitative consistency between parameters of correlation function obtained from NMR and TDDS and their concentration dependence confirm the validity of the qualitative model of the interprotein electrostatic interactions.
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    NMR and dielectric spectroscopy investigation of protein dynamical structure
    (Elsevier, 1990-03) Fedotov, V.; Feldman, Yuri; Krushelnitsky, A. G.; Ermolina, I.
    The general approach to globular proteins dynamical structure investigation by NMR and time domain dielectric spectroscopy (TDDS) is presented. The information on macromolecular dynamical behavior in the case of these two methods is obtained in terms of correlation function and its parameters of atom motions. The interpretation of experimental results in the present work will be carried out in the framework of model-free approach which is common both for magnetic and dielectric relaxation. The lysozyme pH-dependence investigation is presented as an example.
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    The use of TDDS for investigation of structural and dynamic behavior of protein molecules in aqueous solution
    (Elsevier, 1998-06-20) Ermolina, I.; Fedotov, V.; Feldman, Yuri
    The results of the investigation of structure and dynamic behavior of protein in solution by time-domain dielectric spectroscopy are presented. The dipole correlation functions for myoglobin, lysozyme and RNase A solutions at different concentration, pH and temperature were obtained. The processes of the intramolecular interactions of myoglobin molecules, the pH-induced dimerization of lysozyme and thermal denaturation of RNase A are discussed.