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• W1547366876 startingPage "413" @default.
• W1547366876 abstract "Publisher Summary The Forster resonance energy transfer (FRET) and fluorescence lifetime imaging microscopy (FLIM) have emerged as invaluable tools to study and characterize dynamic protein complexes. This chapter explores the FRET–FLIM techniques with particular emphasis on their applications in plant research. The potential use of new donor–acceptor FRET–FLIM pairs and ways of circumventing the problem of chlorophyll autofluorescence, as a likely cause of false FRET signals are also discussed. The most commonly used protocols for expressing fusion proteins transiently or stably in plant cells are described. The chapter presents simple protocols for protoplast transfection and particle bombardment-mediated gene transfer. FRET-based methods have emerged as convenient tools, not only to study protein–protein interactions and/or protein conformational changes, but also to follow the strength and dynamics of these interactions in real time and in different subcellular compartments. FRET remains one of the few available techniques to study in vivo protein dynamics and associations in real time." @default.
• W1547366876 created "2016-06-24" @default.
• W1547366876 creator A5090412070 @default.
• W1547366876 date "2009-01-01" @default.
• W1547366876 modified "2023-09-24" @default.
• W1547366876 title "Chapter 10 FRET and FLIM applications in plants" @default.
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