Molecular dynamics of acetylcholinesterase

Acc Chem Res. 2002 Jun;35(6):332-40. doi: 10.1021/ar010025i.

Abstract

Molecular dynamics simulations are leading to a deeper understanding of the activity of the enzyme acetylcholinesterase. Simulations have shown how breathing motions in the enzyme facilitate the displacement of substrate from the surface of the enzyme to the buried active site. The most recent work points to the complex and spatially extensive nature of such motions and suggests possible modes of regulation of the activity of the enzyme.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Acetylcholinesterase / chemistry*
  • Acetylcholinesterase / metabolism
  • Animals
  • Catalytic Domain
  • Computer Simulation*
  • Humans
  • Motion
  • Protein Binding
  • Protein Conformation
  • Water / chemistry
  • Water / metabolism

Substances

  • Water
  • Acetylcholinesterase