Serine protease acylation proceeds with a subtle re-orientation of the histidine ring at the tetrahedral intermediate

Yanzi Zhou, Yingkai Zhang

Research output: Contribution to journalArticle

Abstract

The acylation mechanism of a prototypical serine protease trypsin and its complete free energy reaction profile have been determined by Born-Oppenheimer ab initio QM/MM molecular dynamics simulations with umbrella sampling.

Original languageEnglish (US)
Pages (from-to)1577-1579
Number of pages3
JournalChemical Communications
Volume47
Issue number5
DOIs
StatePublished - Feb 7 2011

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Acylation
Serine Proteases
Histidine
Trypsin
Free energy
Molecular dynamics
Sampling
Computer simulation
Peptide Hydrolases

ASJC Scopus subject areas

  • Metals and Alloys
  • Materials Chemistry
  • Surfaces, Coatings and Films
  • Electronic, Optical and Magnetic Materials
  • Ceramics and Composites
  • Catalysis
  • Chemistry(all)

Cite this

Serine protease acylation proceeds with a subtle re-orientation of the histidine ring at the tetrahedral intermediate. / Zhou, Yanzi; Zhang, Yingkai.

In: Chemical Communications, Vol. 47, No. 5, 07.02.2011, p. 1577-1579.

Research output: Contribution to journalArticle

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