The time-resolved emission spectra of wild-type green fluorescent protein (wtGFP) and the T203V GFP mutant have been recorded with picosecond time resolution, allowing the separate characterization of the two spectral components associated with the neutral and anionic forms of the GFP chromophore. Significantly, neither component shifts as a function of time. It is suggested that the absence of spectral shift is a result of highly restricted movement of the protein residues in the vicinity of the chromophore. The shapes of the separated spectra are discussed and their relative ratio analyzed in a steady-state analysis.
How to translate text using browser tools
1 March 2006
Time-Resolved Emission Spectra of Green Fluorescent Protein
Andrew A. Jaye,
Deborah Stoner-Ma,
Pavel Matousek,
Michael Towrie,
Peter J. Tonge,
Stephen R. Meech
ACCESS THE FULL ARTICLE
It is not available for individual sale.
This article is only available to subscribers.
It is not available for individual sale.
It is not available for individual sale.
Photochemistry and Photobiology
Vol. 82 • No. 2
March 2006
Vol. 82 • No. 2
March 2006