Direct observation of resonance tryptophan-to-chromophore energy transfer in visible fluorescent proteins

Visible fluorescent proteins from Aequorea victoria contain next to the fluorophoric group a single tryptophan residue. Both molecules form a single donor–acceptor pair for resonance energy transfer (RET) within the protein. Time-resolved fluorescence experiments using tryptophan excitation have sho...

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Bibliographic Details
Published in:Biophysical chemistry 2005-08, Vol.116 (3), p.207-212
Main Authors: Visser, Nina V., Borst, Jan Willem, Hink, Mark A., van Hoek, Arie, Visser, Antonie J.W.G.
Format: Article
Language:English
Subjects:
Anisotropy
anisotropy decays
Cyan fluorescent protein
dynamics
Energy Transfer
Fluorescence anisotropy
Green fluorescent protein
lifetimes
living cells
Luminescent Proteins - chemistry
Models, Molecular
Protein Structure, Tertiary
Resonance energy transfer
single
Spectrometry, Fluorescence
spectroscopy
Time Factors
Time-resolved fluorescence
Tryptophan
Tryptophan - chemistry
Yellow fluorescent protein
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Description
Summary:Visible fluorescent proteins from Aequorea victoria contain next to the fluorophoric group a single tryptophan residue. Both molecules form a single donor–acceptor pair for resonance energy transfer (RET) within the protein. Time-resolved fluorescence experiments using tryptophan excitation have shown that RET is manifested by a distinct growing in of acceptor fluorescence at a rate characteristic for this process. In addition, time-resolved fluorescence anisotropy measurements under the same excitation–emission conditions showed a correlation time that is similar to the time constant of the same RET process with the additional benefit of gaining information on the relative orientation of the corresponding transition dipoles.
ISSN:0301-4622
1873-4200
DOI:10.1016/j.bpc.2005.04.013