Recyclization rate of a photocleaved peptide from multiscale simulation.
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.
Nieber
Harald
H
Lehrstuhl für Theoretische Chemie, Ruhr-Universität Bochum, 44780 Bochum, Germany.
Hellweg
Arnim
A
Doltsinis
Nikos L
NL
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
D009842:Oligopeptides; D011522:Protons