Electrodynamic theory of fluorescence polarization of solutions: theory and application to the determination of protein-protein separation
Applied Optics, Vol. 48, Issue 8, pp. 1553-1564 (2009)
http://dx.doi.org/10.1364/AO.48.001553
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Abstract
The phenomenon of the fluorescence polarization of solutions has found numerous applications in biophysics, biochemistry, immunology, and diagnostic and clinical medicine. The current theory to explain the phenomenon of fluorescence polarization in solutions was developed by F. Perrin in 1926. Perrin based his theory on the belief that fluorescence polarization is a manifestation of rotational Brownian motion. Fluorescence polarization, however, is an electromagnetic radiation phenomenon. Using Maxwell’s equations, suitably modified to account for the quantum behavior of fluorescence, E. Collett developed a theory of fluorescence polarization (the electrodynamic theory) based on a model of dipole–dipole interactions. The electrodynamic theory is used to investigate protein–protein assays to determine the minimum and maximum binding distances between the proteins for (1) an estrogen receptor DNA bound to a fluorescein labeled estrogen response element and (2) a green fluorescent protein chimera of S-peptide (S65T-His6) bound to a free S-protein.
© 2009 Optical Society of America
OCIS Codes
(170.6280) Medical optics and biotechnology : Spectroscopy, fluorescence and luminescence
(260.0260) Physical optics : Physical optics
(260.2510) Physical optics : Fluorescence
(260.5430) Physical optics : Polarization
(300.6280) Spectroscopy : Spectroscopy, fluorescence and luminescence
ToC Category:
Medical Optics and Biotechnology
History
Original Manuscript: September 11, 2008
Revised Manuscript: December 15, 2008
Manuscript Accepted: January 20, 2009
Published: March 5, 2009
Virtual Issues
Vol. 4, Iss. 5 Virtual Journal for Biomedical Optics
Citation
Edward Collett and Beth Schaefer, "Electrodynamic theory of fluorescence polarization of solutions: theory and application to the determination of protein-protein separation," Appl. Opt. 48, 1553-1564 (2009)
http://www.opticsinfobase.org/ao/abstract.cfm?URI=ao-48-8-1553
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