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Contribution of Fluorophores to Protein Kinase C FRET Probe Performance
Author(s) -
Jost Christiane A.,
Reither Gregor,
Hoffmann Carsten,
Schultz Carsten
Publication year - 2008
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200700728
Subject(s) - fluorophore , förster resonance energy transfer , fluorescence , chemistry , biophysics , pleckstrin homology domain , bimolecular fluorescence complementation , green fluorescent protein , monomer , kinase , biochemistry , biology , gene , physics , organic chemistry , quantum mechanics , polymer
Pairing probes : Recently, we prepared several probes that monitor protein kinase C activities in living cells based on a pleckstrin fragment sandwiched between two fluorescent proteins, GFP2 and EYFP. Herein, we replaced the fluorescent proteins (FPs) with monomeric variants which resulted in nonfunctional probes. This suggested that fluorophore dimerization actively participated in probe performance.