Enhanced sensitivity of FRET-based protease sensors by redesign of the GFP dimerization interface

被引：69

作者：

Vinkenborg, Jan L. ^{[1
]}

Evers, Toon H. ^{[1
]}

Reulen, Sanne W. A. ^{[1
]}

Meijer, E. W. ^{[1
]}

Merkx, Maarten ^{[1
]}

机构：

[1] Eindhoven Univ Technol, Dept Biomed Engn, NL-5600 MB Eindhoven, Netherlands

来源：

CHEMBIOCHEM | 2007年 / 8卷 / 10期

关键词：

D O I：

10.1002/cbic.200700109

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

(Graph Presented) 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. © 2007 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

页码：1119 / 1121

页数：3

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