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Proceedings Paper

Recent advances in protein room-temperature phosphorescence spectroscopy
Author(s): Li Sun; Evan R. Kantrowitz; William C. Galley
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Paper Abstract

The use of tryptophan phosphorescence measurements in probing the structural flexibility of globular proteins in solution at room temperature has been limited to date by a number of factors which include: identification of the emitting residues, the low occurrence of tryptophan side chains in sufficiently rigid domains in globular proteins, as well as the absence of a molecular basis for the empirical correlation between phosphorescence lifetimes that are observed at room temperature, and the local viscosity. A review is presented here of our recent work in which we have attempted to address these concerns. A model for the relation between the long- lived triplet lifetimes from buried tryptophan residues and protein flexibility is described along with experimental evidence consistent with the model. Employing site-directed mutagenesis with E.coli alkaline phosphatase, we have both identified the residue responsible for the long-lived emission with the wild-type protein, as well as to reintroduce the indole side chain into alternate relatively inflexible domains resulting in the appearance of RTP.

Paper Details

Date Published: 1 May 1998
PDF: 7 pages
Proc. SPIE 3256, Advances in Optical Biophysics, (1 May 1998); doi: 10.1117/12.307065
Show Author Affiliations
Li Sun, Boston Univ. (United States)
Evan R. Kantrowitz, Boston Univ. (United States)
William C. Galley, McGill Univ. (Canada)

Published in SPIE Proceedings Vol. 3256:
Advances in Optical Biophysics
Joseph R. Lakowicz; J. B. Alexander Ross, Editor(s)

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