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Proceedings Paper

Using 7-azaindole to probe condensed phase dynamics
Author(s): R. L. Rich; F. Gai; Yeh Fong Chen; Jacob Petrich
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Paper Abstract

In order to study experimentally the ultrafast (<1 picosecond to several hundreds of picoseconds) molecular dynamics of protein-protein interactions, an optical probe is required. Tryptophan has been the most widely used intrinsic optical probe of protein structure and dynamics. There are, however, two major problems attendant to the use of tryptophan, especially in fluorescence measurements. First, since tryptophan is a naturally-occurring amino acid there are often several tryptophans in a protein molecule whose emission must be distinguished. Second, the fluorescence decay of tryptophan itself in aqueous solution is nonexponential. We have consequently investigated alternatives to tryptophan. Our work has led us to the amino acid analog, 7-azatryptophan, and its chromophoric moiety, 7-azaindole.

Paper Details

Date Published: 17 August 1994
PDF: 12 pages
Proc. SPIE 2137, Time-Resolved Laser Spectroscopy in Biochemistry IV, (17 August 1994); doi: 10.1117/12.182753
Show Author Affiliations
R. L. Rich, Iowa State Univ. (United States)
F. Gai, Iowa State Univ. (United States)
Yeh Fong Chen, Iowa State Univ. (United States)
Jacob Petrich, Iowa State Univ. (United States)


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

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