1 May 1990 Photophysics of constrained tryptophan derivatives
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Proceedings Volume 1204, Time-Resolved Laser Spectroscopy in Biochemistry II; (1990); doi: 10.1117/12.17693
Event: OE/LASE '90, 1990, Los Angeles, CA, United States
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.
© (1990) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Mary D. Barkley, Luanne F. Tilstra, Lloyd P. McMahon, Marco A. Vela, Mark L. McLaughlin, "Photophysics of constrained tryptophan derivatives", Proc. SPIE 1204, Time-Resolved Laser Spectroscopy in Biochemistry II, (1 May 1990); doi: 10.1117/12.17693; https://doi.org/10.1117/12.17693

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