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Enhanced Sensitivity of FRET‐Based Protease Sensors by Redesign of the GFP Dimerization Interface
Author(s) -
Vinkenborg Jan L.,
Evers Toon H.,
Reulen Sanne W. A.,
Meijer E. W.,
Merkx Maarten
Publication year - 2007
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.200700109
Subject(s) - förster resonance energy transfer , fluorescence , green fluorescent protein , protease , intramolecular force , energy transfer , chemistry , acceptor , interface (matter) , sensitivity (control systems) , biophysics , nanotechnology , biochemistry , materials science , physics , biology , chemical physics , enzyme , gene , stereochemistry , engineering , pulmonary surfactant , gibbs isotherm , quantum mechanics , condensed matter physics , electronic engineering
Close encounters . Sensor proteins based on fluorescence resonance energy transfer (FRET) often display a modest change in emission ratio upon activation. Here, we show that promoting intramolecular interactions between donor and acceptor fluorescent domains is an attractive new strategy for increasing the ratiometric change in FRET‐based protease sensors.