| Abstract
| - The complex transient vibrational spectra of wild type (wt) GFP have been assigned through polarizationanisotropy measurements on isotopically edited proteins. Protein chromophore interactions modify considerablythe vibrational structure, compared to the model chromophore in solution. An excited-state vibrational modeyields information on excited-state electronic structure. The proton relay pathway is characterized in moredetail, and the protonation of the remote E222 residue is shown to occur in a concerted step. Modificationsto protein vibrational modes are shown to occur following electronic excitation, and the potential for these toact as a trigger to the proton relay reaction is discussed.
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