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Phosphorescence of Tryptophan Residues of Proteins at Room Temperature

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Journal of Applied Spectroscopy Aims and scope

Abstract

A brief overview of the results of our works concerned with the study of intramolecular dynamics of proteins by the method of tryptophan phosphorescence at room temperature is given. The mechanisms of quenching tryptophan phosphorescence at room temperature are considered. The lifetimes and quantum yields of tryptophan phosphorescence of proteins at room temperature in different states of aggregation are given. The functional importance of the changes recorded by the phosphorescence method in the intramolecular dynamics of fermented proteins is shown.

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Authors and Affiliations

  1. Institute of Photobiology, National Academy of Sciences of Belarus, 27 Akademicheskaya Str., Minsk, 220072, Belarus

    V. M. Mazhul', E. M. Zaitseva & D. G. Shcherbin

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  1. V. M. Mazhul'
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  2. E. M. Zaitseva
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  3. D. G. Shcherbin
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Correspondence to V. M. Mazhul'.

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Mazhul', V.M., Zaitseva, E.M. & Shcherbin, D.G. Phosphorescence of Tryptophan Residues of Proteins at Room Temperature. Journal of Applied Spectroscopy 69, 213–219 (2002). https://doi.org/10.1023/A:1016180900631

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