Excitation wavelength dependence of the proton-transfer reaction of the green fluorescent protein

Article Abstract:

Picosecond time-correlated single-photon counting was used to measure the proton-transfer rate of green fluorescent protein (GFP) excited by several wavelengths between 266 and 405 nm. It was found that shorter the excitation wavelength, the longer the decay time of the protonated form of the chromophore (ROH) emission band at 450 nm and longer the rise time of the RO(super -) emission band at 512 nm.

Excited state chemistry, Wavelength

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Meta and para effects in the ultrafast excited-state dynamics of the green fluorescent protein chromophores

Article Abstract:

Femtosecond transient absorption and fluorescence upconversion experiments are used for examining the photoinduced dynamics of the meta isomer of the green fluorescent protein chromophore and its O-methylated derivative. The meta compounds have undergone ultrafast intermolecular excited-state proton transfer, which has competed with isomerization, in aqueous solutions.

Analysis, Spectra, Isomerization, Protons, Ultraviolet spectroscopy, Proton capture, Structure

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Study of the long-time fluorescence tail of the green fluorescent protein

Article Abstract:

Two optical techniques are employed to measure the time-resolved optical response of the wild-type green fluorescent protein (WT-GFP) in water and D2O. The results obtained by introducing a mild base into the WT-GFP solution and monitoring its effect on the fluorescence of the ROH form are discussed.

Fluorescence, Proteins

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