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 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.
Visser
Nina V
NV
MicroSpectroscopy Centre, Wageningen University, P.O. Box 8128, 6700 ET Wageningen, The Netherlands. ton.visser@wur.nl
Borst
Jan Willem
JW
Hink
Mark A
MA
van Hoek
Arie
A
Visser
Antonie J W G
AJ
D016880:Anisotropy; D004735:Energy Transfer; D008164:Luminescent Proteins / Q000737:chemistry*; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D013050:Spectrometry, Fluorescence; D013997:Time Factors; D014364:Tryptophan / Q000737:chemistry*
D008164:Luminescent Proteins; D014364:Tryptophan