title: Recyclization rate of a photocleaved peptide from multiscale simulation.
abstract: Unprecedented insight into the phototriggered unfolding of a polypeptide has been gained from a multiscale simulation connecting nonadiabatic ab initio molecular dynamics to classical molecular dynamics in a three-stage manner. An intramolecular H-transfer mechanism that saturates one of the S. radicals of the cleaved S-S bridge and thus prevents recyclization has been observed. This chemical quenching mechanism may be the key to resolving the controversy surrounding the S-S reformation rates.
authors.affiliation: Lehrstuhl für Theoretische Chemie, Ruhr-Universität Bochum, 44780 Bochum, Germany.
authors.forename: Harald
authors.initials: H
authors.lastname: Nieber
authors.forename: Arnim
authors.initials: A
authors.lastname: Hellweg
authors.forename: Nikos L
authors.initials: NL
authors.lastname: Doltsinis
mesh_terms: D000595:Amino Acid Sequence; D003500:Cyclization; D007700:Kinetics; D056004:Molecular Dynamics Simulation; D009842:Oligopeptides / Q000737:chemistry*; D055668:Photochemical Processes; D011487:Protein Conformation; D017510:Protein Folding; D011522:Protons; D011789:Quantum Theory
chemical_list: D009842:Oligopeptides; D011522:Protons