Thesis-1972-King.pdf (2.88 MB)
The low-temperature luminescence of aromatic amino acids in peptides and proteins
thesis
posted on 2018-10-05, 08:26 authored by Leslie A. KingThe 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 KingPublisher 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
1972Notes
A Doctoral Thesis. Submitted in partial fulfilment of the requirements for the award of Doctor of Philosophy at Loughborough University.Language
- en