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

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.

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Bibliografski detalji
Glavni autori: Zhou, Yanzi, Zhang, Yingkai
Format: Artigo
Jezik:Inglês
Izdano: 2010
Teme:
Online pristup:https://ncbi.nlm.nih.gov/pmc/articles/PMC3213857/
https://ncbi.nlm.nih.gov/pubmed/21116528
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1039/c0cc04112b
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