Serine proteases: An ab initio molecular dynamics study

@article{DeSantis1999SerinePA,
  title={Serine proteases: An ab initio molecular dynamics study},
  author={Laura De Santis and Paolo Carloni},
  journal={Proteins: Structure},
  year={1999},
  volume={37}
}
In serine proteases (SPs), the H‐bond between His57 and Asp102 and that between Gly193 and the transition state intermediate play a crucial role in enzymatic function. To shed light on the nature of these interactions, we have carried out ab initio molecular dynamics simulations on complexes representing adducts between the reaction intermediate and elastase (one protein belonging to the SP family). Our calculations indicate the presence of a low‐barrier H‐bond between His57 and Asp102, in… 

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