Enhanced Sensitivity of FRET‐Based Protease Sensors by Redesign of the GFP Dimerization Interface

Abstract

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. Supporting information for this article is available on the WWW under http://www.wiley-vch.de/contents/jc_2268/2007/z700109_s.pdf or from the author. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.