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The low-temperature luminescence of aromatic amino acids in peptides and proteins

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posted on 05.10.2018 by Leslie A. King
The aromatic amino acids, tryptophan and tyrosine exhibited fluorescence and phosphorescence at 77°K; phenylalanine was found to be non-luminescent. The luminescence elf peptides and proteins containing tryptophan was dominated by that amino acid. In general, tyrosine emission was only observed in the absence of tryptophan. This effect is explained in terms of energy transfer from the excited singlet state of tyrosine to tryptophan. The luminescence characteristics of tryptophan and tyrosine were sensitive to numerous environmental factors. In polar media and in the vicinity of a tyrosinate anion, the relative phosphorescence quantum yield of tryptophan was enhanced. The reverse occurred in apolar media. In addition, the excited states of tryptophan and tyrosine were perturbed by a heavy atom effect. [Continues.]

Funding

Science Research Council (studentship no. 70/491).

History

School

  • Science

Department

  • Chemistry

Publisher

© Leslie Albert King

Publisher statement

This work is made available according to the conditions of the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) licence. Full details of this licence are available at: https://creativecommons.org/licenses/by-nc-nd/4.0/

Publication date

1972

Notes

A Doctoral Thesis. Submitted in partial fulfilment of the requirements for the award of Doctor of Philosophy at Loughborough University.

Language

en

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