Nanosecond relaxation dynamics of protein GB1 identified by the time-dependent red shift in the fluorescence of tryptophan and 5-Fluorotryptophan

Article Abstract:

The time-resolved fluorescence of the wild-type B1 domain of Streptococcal protein G (GB1) and its 5-fluorotryptophan (5FTrp) variant at more than 30 different emission wave lengths between 300 and 470 nm exhibits no signs of static heterogeneity but show the time-dependent red shift characteristic of microscopic dielectric relaxation. It is verified that time-dependent red shifts in the fluorescence of 5 FTrp and unmodified Trp are identical and caused by the relaxation of the protein matrix and not by fluorophore itself.

Fluorescence, Bacterial proteins, Tryptophan

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A study of the time-resolved fluorescence spectrum and red edge effect of ANF in a room-temperature ionic liquid

Article Abstract:

The time and wavelength-dependent emission spectra of 2-amino-7-nitrofluorene (ANF) in 1-butyl-3-methylimidazolium hexafluorophosphate ([[BMIM.sup.+]])([P[F6.sup.-]]) are predicted. Electronic photoexcitation of ANF dissolved in ([[BMIM.sup.+]])([P[F6.sup.-]]) results in an absorption wavelength dependent emission spectrum, that is, if excitation is on the blue (red) end of the absorption spectrum, emission also appears to shift to the blue (red).

Optical properties, Wavelength

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How does water affect the dynamics of the room-temperature ionic liquid 1-hexyl-3-methylimidazolium hexafluorophosphate and the fluorescence spectroscopy of coumarin-153 when dissolved in it?

Article Abstract:

Molecular dynamics simulations of mixtures of 1-hexyl-3-methylimidazolium hexafluorophosphate and water are performed in order to examine how small amounts of water affect the translational and rotational dynamics of this ionic liquid (IL). Excitation wavelength-dependent emission is seen both in the neat IL and in the IL+water mixture.

Phosphates, Water, Ionic solutions, Fluorescence spectroscopy, Mechanical properties

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