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Proceedings Paper

Photophysics of constrained tryptophan derivatives
Author(s): Mary D. Barkley; Luanne F. Tilstra; Lloyd P. McMahon; Marco A. Vela; Mark L. McLaughlin
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Paper Abstract

The aromatic amino acid tryptophan is widely used as an intrinsic fluorescent probe of the solution conformation and dynamics of peptides and proteins. However, its complex photophysics makes it difficult to interpret the fluorescence results. The biexponential fluorescence decay of the tryptophan zwitterion is presumed to be due to ground-state rotamers. Intramolecular proton and electron transfer reactions involving the excited indole ring and amino acid functional groups have been proposed to account for the lifetime differences among rotamers. Excited-state H-D exchange occurs at the C-4 position of indole. In the proposed mechanism for the photosubstitution reaction, the ammonium group loops back over the aromatic ring and assists the proton exchange.

Paper Details

Date Published: 1 May 1990
PDF: 2 pages
Proc. SPIE 1204, Time-Resolved Laser Spectroscopy in Biochemistry II, (1 May 1990); doi: 10.1117/12.17693
Show Author Affiliations
Mary D. Barkley, Louisiana State Univ. (United States)
Luanne F. Tilstra, Louisiana State Univ. (United States)
Lloyd P. McMahon, Louisiana State Univ. (United States)
Marco A. Vela, Louisiana State Univ. (United States)
Mark L. McLaughlin, Louisiana State Univ. (United States)


Published in SPIE Proceedings Vol. 1204:
Time-Resolved Laser Spectroscopy in Biochemistry II
Joseph R. Lakowicz, Editor(s)

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