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Proceedings Paper

Anisotropy Decays Of Single Tryptophan Proteins Measured By Ghz Frequency-Domain Fluorometry With Collisional Quenching
Author(s): Joseph R Lakowicz; Ignacy Gryczynski; Henryk Szmacinaski; Henryk Cherek; Nanda Joshi
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Paper Abstract

We use frequency-domain fluorometry to determine the anisotropy decays of the tryptophan emission from S. nuclease and from the model compound gly-trp-gly. Resolution of the rapid and complex anisotropy decays was enhanced by global analysis of the data measured in the presence of quenching by either oxygen or acrylamide. Data were obtained at four to six quencher concentrations, and the data analyzed globally to recover the anisotropy decay. Because the decay times were decreased by quenching, measurements were possible to a upper frequency limit of 2 GHz. The anisotropy decay of gly-trp-gly revealed 40 ps of the indole ring, which was resolved from the overall 150 ps correlation times of the tripeptide. The anisotropy decay of nuclease displayed a 90/ps component as well as a 10 ns component due to overall rotational diffusion. We believe these highly resolved anisotropy decays are suitably for comparison with molecular dynamic simulations.

Paper Details

Date Published: 24 June 1988
PDF: 8 pages
Proc. SPIE 0909, Time-Resolved Laser Spectroscopy in Biochemistry, (24 June 1988); doi: 10.1117/12.945384
Show Author Affiliations
Joseph R Lakowicz, University of Maryland at Baltimore (United States)
Ignacy Gryczynski, University of Maryland at Baltimore (United States)
Henryk Szmacinaski, University of Maryland at Baltimore (United States)
Henryk Cherek, University of Maryland at Baltimore (United States)
Nanda Joshi, University of Maryland at Baltimore (United States)

Published in SPIE Proceedings Vol. 0909:
Time-Resolved Laser Spectroscopy in Biochemistry
Joseph R. Lakowicz, Editor(s)

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