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Proceedings Paper

Studies of tryptophan fluorescence using bacteriophage T4 lysozyme
Author(s): Bruce S. Hudson
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Paper Abstract

The nature of the complex fluorescence of the indole chromophore of tryptophan is briefly reviewed. A recent molecular dynamics simulation of the relaxation of water surrounding the excited state of tryptophan demonstrates that this 'dielectric relaxation' aspect of tryptophan photophysics is well-understood. The relationship of this behavior in solutions to the photophysics of tryptophan in proteins is discussed. Another well-known feature of tryptophan fluorescence is the ability of a variety of 'collisional quenchers' to reduce the emission yield and lifetime. The relevance of this aspect of the photophysics of tryptophan to protein luminescence is also discussed.

Paper Details

Date Published: 17 June 1993
PDF: 10 pages
Proc. SPIE 1921, Laser Spectroscopy of Biomolecules, (17 June 1993); doi: 10.1117/12.146117
Show Author Affiliations
Bruce S. Hudson, Univ. of Oregon (United States)

Published in SPIE Proceedings Vol. 1921:
Laser Spectroscopy of Biomolecules
Jouko E. Korppi-Tommola, Editor(s)

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