Tseyslyer Y. The influence of extremely low frequency mag-netic field on structurally-functional properties of globular proteins

The dissertation is devoted to studying of changes of structural functional characteristics of some globular proteins under the influence of the extremely low frequency magnetic field (MF) in solutions of the native proteins and in conditions of saturation of proteins by hydrophobic ligands - chloroform and benzol. Such methods have been used: the method of modulation of MF, the method of false influence of MF; methods absorption and differential spectroscopy, analytical electrophoresis, fluorescent methods, methods of denaturation and renaturatsion of protein, definition of activity of enzymes, standard mathematical methods of variational statistics. It is shown, that MF does not influence of absorption spectra of proteins from various structural classes, but influence is ob-served on own fluorescence of albumin depending on fre-quency of MF. Influence of MF on structurally functional properties of proteins stronger at interaction with hydrophobic ligands. MF change adsorption of hydrophobic substances by proteins macromolecules and also their dynamics of confor-mation transitions.