[Role of rapid movement of spin labels in interpreting EPR spectra for spin-labelled macromolecules].

The method of spin labeling was used to monitor quick movements of side residues in protein monocrystals. The EPR spectra of monocrystals of spin-labeled lysozyme at different orientations of the tetrahonal crystal relative to the direction of the magnetic field were interpreted using the molecular dynamics method. A simple model was proposed, which enables one to calculate the trajectory of movements of the spin label by the molecular dynamic method over a relatively short period of time.

[Effect of various humidity on local dynamic structure of lysozyme in a spin-labeled tetragonal crystal].

The dynamics of the side groups of amino acid residues and local conformational changes in the lysozyme molecule upon dehydration and rehydration of lysozyme crystals were studied by the methods of spin label, X-ray diffraction, and molecular dynamics. The His15 residue of lysozyme from chicken egg white was modified by spin label, and spin-labeled tetragonal crystals of the protein were grown. The spatial structure of the covalently bound spin label and its immediate surroundings in the lysozyme tetragonal crystal was determined.

[Spin-spin interaction upon introduction of a spin label into immunoglobulins M and G at the carbohydrate moiety].

By spin labeling the monoclonal IgM and normal IgG at the carbohydrate moiety with 2,2,6,6-tetramethyl-4-aminopiperidine-1-oxyl, preparations were obtained whose ESR spectra indicate rapid exchange spin-spin interactions between two spin labels. It was shown that, in the case of spin-labeled IgM, this spectrum is determined by a glycopeptide noncovalently bound to IgM, which incorporates two spin labels.