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Proceedings Paper

Investigation Of Conformational Changes In Proteins Using Fluorescence And Fluorescence Anisotropy Decay
Author(s): John M Brewer; Phillippe Bastiaens; John Lee
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Paper Abstract

Several well-characterized conformational changes in two proteins, bovine serum albumin and yeast enolase, were investigated using steady-state quenching and dynamic fluorescence measurements. These results were compared with published observations. Conformational changes involving domain or subunit separation are associated with increased Stern-Volmer quenching constants but no consistent change in emission maximum or average tryptophanyl-fluorescence lifetime. Rotational correlation times from tryptophanyl-fluorescence anisotropy decay are in agreement with expected values, showing the value of such measurements in analysis of conformational changes in proteins.

Paper Details

Date Published: 24 June 1988
PDF: 5 pages
Proc. SPIE 0909, Time-Resolved Laser Spectroscopy in Biochemistry, (24 June 1988); doi: 10.1117/12.945380
Show Author Affiliations
John M Brewer, University of Georgia (United States)
Phillippe Bastiaens, University of Georgia (United States)
John Lee, University of Georgia (United States)

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

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