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ANALYTICAL DESCRIPTION OF LOW-TEMPERATURE TRYPTOPHAN LUMINESCENCE IN PROTEINS ON BASE OF PHYSICAL MODEL

By Gintaras Yuventsievich Deikus and Russian Academy of Sciences (Russian Federation) The Institute of Biological Instrument Making

Abstract

The theoretical-experimental approach based on the theory of electron-vibrational interaction of the multiatom molecules has been applied to the analysis of the spectra for tryptophan luminescence of the proteins measured at temperature 77 K. It has been shown firstly that the structurized phosphorescence and fluorence spectra of the tryptophan residues in the proteins are described well on base of the physical model supposing the revealing of two independent vibrations in these spectra. The analytical description of such spectra increases the number of the parameters characterizing the spectrum at low temperatures. The sensitivity of such parameters to changing information state of the protein has been demonstrated firstly, and thus the expediency of the low-temperature tryptophan luminescence use in the investigation of the state and structural transitions in the proteins has been confirmed. Usage field: molecular biophysics.Available from VNTIC / VNTIC - Scientific & Technical Information Centre of RussiaSIGLERURussian Federatio

Topics: 07C - Organic chemistry, 06Y - Biophysics, SPECTRA, LOW-TEMPERATURE TRYPTOPHAN LUMINESCENCE, PROTEINS, PHYSICAL MODELS
Year: 1997
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Provided by: OpenGrey Repository
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