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Proceedings Paper

Evidence for reversible excited-state process in tryptophan zwitterion
Author(s): Noel Boens; Luc Van Dommelen; Frans C. De Schryver; Marcel Ameloot
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Paper Abstract

This report gives evidence that the biexponential fluorescence decay of tryptophan zwitterion in H2O solution is due to the occurrence of a reversible two-state excited-state process whereby the corresponding ground-state species are excited. The rate constants are within the intervals: 0<k01<0.57(ns)-1, 0.76(ns)-1<k21<1.33(ns)-1, 0<k02<0.58(ns)-1, 0.77(ns)-1<k12<1.35(ns)-1. These limits were calculated using the values for S1 equals k01 + k21 (1.33+/- 0.01(ns)-1), S2 equals k02 + k12(1.35+/- 0.01(ns)-1), and P equals k21k12(1.03+/- 0.01(ns)-2). The emission spectra of the two excited-state species can be uniquely determined and are different from those associated with the decay times. These results were obtained by repetitive global compartmental analyses of the fluorescence decay surface of tryptophan zwitterion measured over the entire emission spectrum as a function of quencher concentration. This new and powerful analysis method is applicable to all biexponential protein fluorescence decays.

Paper Details

Date Published: 17 August 1994
PDF: 12 pages
Proc. SPIE 2137, Time-Resolved Laser Spectroscopy in Biochemistry IV, (17 August 1994); doi: 10.1117/12.182749
Show Author Affiliations
Noel Boens, Katholieke Univ. Leuven (Belgium)
Luc Van Dommelen, Katholieke Univ. Leuven (Belgium)
Frans C. De Schryver, Katholieke Univ. Leuven (Belgium)
Marcel Ameloot, Limburgs Univ. Centrum (Belgium)


Published in SPIE Proceedings Vol. 2137:
Time-Resolved Laser Spectroscopy in Biochemistry IV
Joseph R. Lakowicz, Editor(s)

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