Investigation Of Conformational Changes In Proteins Using Fluorescence And Fluorescence Anisotropy Decay

John M Brewer; Phillippe Bastiaens; John Lee

doi:10.1117/12.945380

24 June 1988 Investigation Of Conformational Changes In Proteins Using Fluorescence And Fluorescence Anisotropy Decay

John M Brewer, Phillippe Bastiaens, John Lee

Proceedings Volume 0909, Time-Resolved Laser Spectroscopy in Biochemistry; (1988) https://doi.org/10.1117/12.945380
Event: 1988 Los Angeles Symposium: O-E/LASE '88, 1988, Los Angeles, CA, United States

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.

Citation Download Citation

John M Brewer, Phillippe Bastiaens, and John Lee "Investigation Of Conformational Changes In Proteins Using Fluorescence And Fluorescence Anisotropy Decay", Proc. SPIE 0909, Time-Resolved Laser Spectroscopy in Biochemistry, (24 June 1988); https://doi.org/10.1117/12.945380

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