title: Efficient excited-state deactivation of the Gly-Phe-Ala tripeptide via an electron-driven proton-transfer process.
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.
authors.affiliation: Department of Chemistry, Technische Universitat Munchen, D-85747 Garching, Germany. dorit.shemesh@ch.tum.de
authors.forename: Dorit
authors.initials: D
authors.lastname: Shemesh
authors.forename: Andrzej L
authors.initials: AL
authors.lastname: Sobolewski
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Domcke
mesh_terms: D004583:Electrons; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D011522:Protons
chemical_list: D010455:Peptides; D011522:Protons