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• W1978178258 abstract "One of the most promising imaging techniques for monitoring dynamic protein interactions in living cells with optical microscopy, universally referred to as FRET, employs the non-radiative transfer of energy between two closely adjacent spectrally active molecules, often fluorescent proteins. The use of FRET in cell biology has expanded to such a degree that hundreds of papers are now published each year using biosensors to monitor a wide spectrum of intracellular processes. Most of these sensors sandwich an environmentally active peptide between cyan and yellow fluorescent protein (CFP and YFP) derivatives to assay variables such as pH, calcium ion concentration, enzyme activity, or membrane potential. The availability of these sensitive indicators is growing rapidly, but many are hampered by a low dynamic range that often is only marginally detectable over the system noise. Furthermore, extended periods of excitation at wavelengths below 500 nm have the potential to induce phototoxic effects that can mask or alter the biological events under observation. Recent success in expanding the fluorescent protein color palette offers the opportunity to explore new FRET partners that may be suitable for use in advanced biosensors." @default.
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• W1978178258 date "2008-02-07" @default.
• W1978178258 modified "2023-09-23" @default.
• W1978178258 title "Searching the fluorescent protein color palette for new FRET pairs" @default.
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• W1978178258 doi "https://doi.org/10.1117/12.764560" @default.
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