Abstract
A new approach for the investigation of intramolecular motions in proteins, based on the study of spin-lattice relaxation of the iron atom of the protein active centres, has been developed. The gamma-resonance spectra have been obtained for the globules of transferrin enriched with57Fe. They possessed a paramagnetic hyperfine structure up to room temperature. This afforded the opportunity to experimentally investigate high temperature conformational motions in proteins and to study their influence on the spin-lattice relaxation. A theoretical model of relaxational spectra calculations has been developed, which enabled us to extract the frequency distribution of the spin-lattice relaxation from the shape of the spectra. The approach developed for the study of intramolecular dynamics of proteins based on the examination of spin-lattice relaxation in gamma-resonance spectra increases the frequency scale by at least one order in comparison with conventional methods.
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