Journal
CHEMICAL PHYSICS LETTERS
Volume 482, Issue 1-3, Pages 38-43Publisher
ELSEVIER
DOI: 10.1016/j.cplett.2009.09.087
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Funding
- Deutsche Forschungsgemeinschaft
- Alexander von Humboldt foundation
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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. (C) 2009 Elsevier B. V. All rights reserved.
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