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Probing the Active Site of Acetylcholinesterase by Molecular Dynamics of Its Phosphonate Ester Adducts †

Bencsura, Akos ; Enyedy, Istvan Y. ; Kovach, Ildiko M.

Journal of the American Chemical Society, 01/1996, Vol.118(36), pp.8531-8541 [Peer Reviewed Journal]

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  • Title:
    Probing the Active Site of Acetylcholinesterase by Molecular Dynamics of Its Phosphonate Ester Adducts †
  • Author: Bencsura, Akos ; Enyedy, Istvan Y. ; Kovach, Ildiko M.
  • Description: The molecular dynamics (MD) simulations of the optimized structures of native Torpedo californica acetylcholinesterase (AChE) and its adducts are described. According to an analysis of the MD simulation of AChE, there is a tight catalytic triad already 'wound' in the reactant state to act on the substrate. The H-bond distance between His440 and Glu327 increases by ~10% as skeletal motions are allowed. These MD simulations provide insight into how the skeletal motions accommodate an overcrowded active site, especially in the pentacoordinate adduct.
  • Is Part Of: Journal of the American Chemical Society, 01/1996, Vol.118(36), pp.8531-8541
  • Identifier: ISSN: 0002-7863 ; E-ISSN: 1520-5126 ; DOI: http://dx.doi.org/10.1021/ja952406v
  • Subjects: Acetylcholinesterase -- Analysis ; Molecular Dynamics -- Usage ; Phosphonates -- Analysis
  • Language: English
  • Source: American Chemical Society (via CrossRef)

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