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• W2483626464 abstract "Far-red fluorescent proteins are critical for in vivo imaging applications, but the relative importance of structure versus dynamics in generating large Stokes-shifted emission is unclear. The unusually red-shifted emission of TagRFP675, a derivative of mKate, has been attributed to the multiple hydrogen bonds with the chromophore N-acylimine carbonyl. We characterized TagRFP675 and point mutants designed to perturb these hydrogen bonds with spectrally resolved transient grating and time-resolved fluorescence (TRF) spectroscopies supported by molecular dynamics simulations. TRF results for TagRFP675 and the mKate/M41Q variant show picosecond time scale red-shifts followed by nanosecond time blue-shifts. Global analysis of the TRF spectra reveals spectrally distinct emitting states that do not interconvert during the S1 lifetime. These dynamics originate from photoexcitation of a mixed ground-state population of acylimine hydrogen bond conformers. Strategically tuning the chromophore environment in TagRFP675 might stabilize the most red-shifted conformation and result in a variant with a larger Stokes shift." @default.
• W2483626464 created "2016-08-23" @default.
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• W2483626464 date "2016-07-27" @default.
• W2483626464 modified "2023-10-15" @default.
• W2483626464 title "Fluorescence from Multiple Chromophore Hydrogen-Bonding States in the Far-Red Protein TagRFP675" @default.
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• W2483626464 doi "https://doi.org/10.1021/acs.jpclett.6b01172" @default.
• W2483626464 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5004773" @default.
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