Recyclization rate of a photocleaved peptide from multiscale simulation

J Am Chem Soc. 2010 Feb 17;132(6):1778-9. doi: 10.1021/ja9100497.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cyclization
  • Kinetics
  • Molecular Dynamics Simulation*
  • Oligopeptides / chemistry*
  • Photochemical Processes*
  • Protein Conformation
  • Protein Folding
  • Protons
  • Quantum Theory

Substances

  • Oligopeptides
  • Protons