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Cover Picture: Monitoring Protein Interactions in the Living Cell Through the Fluorescence Decays of the Cyan Fluorescent Protein (ChemPhysChem 7/2006)
Author(s) -
Grailhe Regis,
Merola Fabienne,
Ridard Jacqueline,
Couvignou Stephen,
Le Poupon Chantal,
Changeux JeanPierre,
LaguittonPasquier Helene
Publication year - 2006
Publication title -
chemphyschem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.200690022
Subject(s) - cyan , förster resonance energy transfer , fluorescence , yellow fluorescent protein , bimolecular fluorescence complementation , green fluorescent protein , fluorescent protein , chemistry , biophysics , dimer , resonant inductive coupling , photochemistry , crystallography , energy transfer , biology , biochemistry , chemical physics , physics , optics , gene , organic chemistry , quantum mechanics
The cover picture shows how the fluorescence decays of the cyan fluorescent protein (CFP) can reveal molecular interactions and organisation in the living cell. Förster resonant energy transfer (FRET) towards its acceptor, the yellow fluorescent protein (YFP), leads to charateristic decreases in the CFP fluorescence lifetimes. Despite the very high intracellular protein concentrations achieved, leading to strong molecular proximity, the results show that CFP and YFP fail to form inside the cell the dimer, previously observed for purified green fluorescent proteins. Find out more in the Article by Grailhe et al. on page 1442.