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- W2044948239 abstract "The excited-state potential-energy surfaces of the lowest-energy conformer of the tryptophan–glycine dipeptide have been investigated with ab initio electronic-structure methods. The calculations reveal a potentially very efficient excited-state deactivation mechanism via conical intersections of the excited states of the indole chromophore with locally-excited and charge-transfer states of the peptide backbone. These findings suggest that the excited-state lifetime of the lowest-energy conformer of the Trp-Gly dipeptide may be too short to allow the detection of a resonant two-photon ionization signal. It is proposed that the efficient excited-state deactivation enhances the photostability of the dipeptide." @default.
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- W2044948239 date "2009-11-01" @default.
- W2044948239 modified "2023-09-25" @default.
- W2044948239 title "Photophysics of the Trp-Gly dipeptide: Role of electron and proton transfer processes for efficient excited-state deactivation" @default.
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- W2044948239 doi "https://doi.org/10.1016/j.cplett.2009.09.087" @default.
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