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- W2038012586 abstract "In recent years, spectral relaxation has been established as a theory to explain nonexponential decays of intrinsic tryptophan fluorescence in single-tryptophan proteins. However, systematic measurements are required to account for the occurence of spectral relaxation in specific proteins. We investigated different single tryptophan proteins, varying in size, predominating secondary structure and polarity of the fluorophor environment, in order to correlate these parameters with spectral relaxation.Multidimensional static fluorescence measurements delivers a spectroscopic fingerprint containing every single excitation and emission spectrum of the substance in question. Herewith we evaluated stokes shifts, quantum yields and stern vollmer constants, yielding information on the polarity, accessability and quenching acitivity of the fluorophor environment. Furthermore, shifts in emission wavelength at the red excitation edge indicated the presence of a relaxation process.Fluorescence dynamics were investigated using a tunable pulsed laser (either 3 or 80ps pulse width) and an intensified streak camera as detection unit, yielding simultaneously time and wavelength resolved spectra. Detection efficiencies of the phosphorus screen were calibrated via a halogen lamp and the accuracy of the resulting lifetimes was confirmed using a matrix of different reference dyes.The resulting measurements revealed the occurrence of spectral relaxation due to shifts of the center of gravity with time and increase of lifetime with emission wavelength. Though negative preexponential factors could only rarely be assigned, an increasing time shift of the fluorescence maximum at longer emission wavelength proved these effects to stem from an excited state process and not from different conformers in the ground state." @default.
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- W2038012586 date "2009-02-01" @default.
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- W2038012586 title "Investigation Of Excited-State Relaxation In Single-Tryptophan-And Other Proteins Via Multidimensional Static And Time-Resolved Fluorescence" @default.
- W2038012586 doi "https://doi.org/10.1016/j.bpj.2008.12.136" @default.
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