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"Excited-state dynamics of bacteriorhodopsin probed by broadband femtosecond fluorescence spectroscopy" B. Schmidt, C. Sobotta, B. Heinz, S. Laimgruber, M. Braun, P. GilchBiochimica et Biophysica Acta 1706 (2005) 165-173 Abstract: The impact of varying excitation densities (~0.3 to ~40 photons per molecule) on the ultrafast fluorescence dynamics of bacteriorhodopsin has been studied in a wide spectral range (630–900 nm). For low excitation densities, the fluorescence dynamics can be approximated biexponentially with time constants of ~0.15 and ~0.45 ps. The spectrum associated with the fastest time constant peaks at 650 nm, while the 0.45 ps component is most prominent at 750 nm. Superimposed on these kinetics is a shift of the fluorescence maximum with time (dynamic Stokes shift). Higher excitation densities alter the time constants and their amplitudes. These changes are assigned to multi-photon absorptions. BMO authors (in alphabetic order): Markus Braun Peter Gilch Bjoern Heinz Stefan Laimgruber Bernhard Schmidt Constanze Sobotta Assoziierte Projekte: Spectroscopy of the functional dynamics of proteins Ultrafast Fluorescence Spectroscopy - The Kerr-Gate Setup  WWW-Version |