Issue 5, 2011
From the journal:

Chemical Communications

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

Yanzi Zhoua  and  Yingkai Zhang*a  

* Corresponding authors

a Department of Chemistry, New York University, New York, USA
E-mail: yingkai.zhang@nyu.edu
Tel: +1 212-998-7882

Abstract

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

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

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Article information

DOI
https://doi.org/10.1039/C0CC04112B
Article type
Communication
Submitted
28 Sep 2010
Accepted
12 Nov 2010
First published
29 Nov 2010

Chem. Commun., 2011,47, 1577-1579

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

Y. Zhou and Y. Zhang, Chem. Commun., 2011, 47, 1577 DOI: 10.1039/C0CC04112B

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