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Abstract
Ab initio electronic-structure calculations indicate a mechanism for efficient excited-state deactivation of a low-energy conformer of the Gly-Phe-Ala tripeptide. The particularly short excited-state lifetime can explain the unexpected absence of this conformer in resonant two-photon ionization spectra. It is suggested that these ultrafast electronic deactivation processes provide specific conformers of peptides with a high degree of photostability.
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