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Spin-lattice relaxation and intramolecular motions in transferrin on the Mössbauer spectroscopy data

Hyperfine Interactions, ISSN: 0304-3834, Vol: 91, Issue: 1, Page: 923-929
1994
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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 withFe. 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. © 1994 J.C. Baltzer AG, Science Publishers.

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