Chemical Physics 237 (1998) 183-193
Kummer, A.D., Kompa, C., Lossau, H., Pöllinger-Dammer, F., Michel-Beyerle, M.E., Silva, C.M., Bylina, E.J., Coleman, W.J., Yang, M.M., and Youvan, D.C.
Institut für Physikalische und Theoretische Chemie, Technische Universität München, D-85748 Garching, Germany.
KAIROS Scientific Inc., 3350 Scott Blvd., Bldg. 62, Santa Clara, CA 95054, USA
Steady-state absorption and fluorescence excitation spectra together with ps-fluorescence and fs-absorption measurements have identified an important relaxation channel of excited states in Green Fluorescent Protein (GFP). GFP derivatives with (1) shortened lifetimes of the protonated chromophore RH* state and the deprotonated chromophore R¯* state, and (2) rapid recovery of the RH or R¯ ground state have been isolated and characterized. These shortened excited state lifetimes and fast ground state recovery are interpreted in terms of internal conversion induced by torsional motion within the chromophore.
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