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  Photochromicity and fluorescence lifetimes of green fluorescent protein

Striker, G., Subramaniam, V., Seidel, C., & Volkmer, A. (1999). Photochromicity and fluorescence lifetimes of green fluorescent protein. Journal of Physical Chemistry B, 103, 8612-8617.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-FBCB-6 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-922B-6
Genre: Journal Article

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 Creators:
Striker, G.1, Author              
Subramaniam, V.1, Author              
Seidel, C.2, Author              
Volkmer, A., Author
Affiliations:
1Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society, ou_578628              
2Department of Spectroscopy and Photochemical Kinetics, MPI for biophysical chemistry, Max Planck Society, ou_578624              

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Free keywords: Excitation; Microscopy
 Abstract: The green fluorescent protein (GFP) of the bioluminescent jellyfish Aequorea and its mutants have gained widespread usage as an indicator of structure and function within cells. Proton transfer has been implicated in the complex photophysics of the wild-type molecule, exhibiting a protonated A species excited at 400 nm, and two deprotonated excited-state species I* and B* with red-shifted excitation similar to 475 nm. Photochromicity between the protonated and deprotonated species has been reported upon 400 nm excitation. Using precise time-resolved spectroscopy, we have been able to distinguish the fluorescence lifetimes of the I and B species (similar to 3.3 and similar to 2.8 ns, respectively) and show that the irreversible photochromicity which we observe is due to formation in the excited state of the B species, which cannot return to other species in the ground state. The ground state A and I species are in thermal equilibrium. Anistropy measurements indicate chat the chromophore lies rigidly in the molecule with a rotational correlation time of similar to 15.5 ns, as is to be expected for a molecule of this size. Time-resolved measurements of enhanced yellow fluorescent protein (EYFP) and red-shifted green fluorescent protein (RSGFP) were also analyzed.

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Language(s): eng - English
 Dates: 2005-08-051999
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: -
 Identifiers: eDoc: 236978
Other: 11563
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Title: Journal of Physical Chemistry B
Source Genre: Journal
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Pages: - Volume / Issue: 103 Sequence Number: - Start / End Page: 8612 - 8617 Identifier: -