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Proceedings Paper

Time-resolved fluorescence studies of the protein folding process: new instrumentation, analysis, and experimental approaches
Author(s): Joseph M. Beechem; Elizabeth A. James; Ludwig Brand
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Paper Abstract

Utilizing time-resolved fluorescence techniques for the examination of the protein folding problem requires the development of some new methods of data acquisition, analysis, and experimental design. Structural information (rotational relaxation times, intramolecular distance distributions, conformational dynamics) need to be obtained on transient non-equilibrium species which may exist for as little as tens of milliseconds. In this report, the development of a stopped-flow timeresolved fluorometer is described. In addition, a unique molecular genetic system developed for the protein Stapholococcal Nuclease is utilized to assist in the placement of donor/acceptor pairs in strategic locations throughout the protein. Combining these two projects together, provides the potential for determining the structural details involved in the folding (unfolding) behavior in this protein.

Paper Details

Date Published: 1 May 1990
PDF: 13 pages
Proc. SPIE 1204, Time-Resolved Laser Spectroscopy in Biochemistry II, (1 May 1990); doi: 10.1117/12.17715
Show Author Affiliations
Joseph M. Beechem, Vanderbilt Univ. (United States)
Elizabeth A. James, Johns Hopkins Univ. (United States)
Ludwig Brand, Johns Hopkins Univ. (United States)

Published in SPIE Proceedings Vol. 1204:
Time-Resolved Laser Spectroscopy in Biochemistry II
Joseph R. Lakowicz, Editor(s)

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