Proceedings Paper
Investigation Of Conformational Changes In Proteins Using Fluorescence And Fluorescence Anisotropy Decay| Format | Member Price | Non-Member Price |
|---|---|---|
| $17.00 | $21.00 |
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
Published in SPIE Proceedings Vol. 0909:
Time-Resolved Laser Spectroscopy in Biochemistry
Joseph R. Lakowicz, Editor(s)
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)
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)
© SPIE. Terms of Use
