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