Photophysics of green and red fluorescent proteins: implications for quantitative microscopy


This chapter describes the implications for quantitative microscopy. The green fluorescent protein (GFP) from the jellyfish Aequorea victoria and its mutants constitute a class of fluorophores that has revolutionized the evaluation of molecular interactions and visualization of biological systems. When fused to proteins of interest and expressed in vivo, fluorescent proteins (FPs) act as versatile indicators of structure and function within cells and can be imaged with the full repertoire of fluorescence microscopy techniques. FPs and their constructs are finding increasing use in fluorescence lifetime imaging microscopy (FLIM) and fluorescence resonance energy transfer (FRET) modes of microspectroscopy for the elucidation of protein-protein interactions, signaling, and trafficking in cellular systems. The simple and the most common, application of FPs is as a passive marker fused to a target protein of interest for visualizing its spatiotemporal distribution. Mutations in and around the chromophore have systematic effects on the spectra. Green and red fluorescent proteins exhibit photophysical properties that are generally more complex than those of traditional fluorophores, for example, fluorescein and rhodamine

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oai:vtl.cc.swin.edu.au:swin:33999Last time updated on 5/26/2016

This paper was published in Swinburne Research Bank.

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