Electrostatic steering of substrate to acetylcholinesterase: analysis of field fluctuations.

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  • Author(s): Wlodek ST;Wlodek ST; Shen T; McCammon JA
  • Source:
    Biopolymers [Biopolymers] 2000 Mar; Vol. 53 (3), pp. 265-71.
  • Publication Type:
    Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Wiley Country of Publication: United States NLM ID: 0372525 Publication Model: Print Cited Medium: Print ISSN: 0006-3525 (Print) Linking ISSN: 00063525 NLM ISO Abbreviation: Biopolymers Subsets: MEDLINE
    • Publication Information:
      Original Publication: New York, NY : Wiley
    • Subject Terms:
      Acetylcholinesterase/*chemistry; Electrochemistry ; Protein Structure, Quaternary ; Static Electricity ; Substrate Specificity
    • Abstract:
      Based on previous molecular dynamics simulation results for acetylcholinesterase dimer, we calculate and analyse the electrostatic field fluctuations around the enzyme. The results show that dynamic features of the electrostatic field favor attraction of the positively-charged substrate. An Internet link to an animation of the results is also provided.
      (Copyright 2000 John Wiley & Sons, Inc.)
    • Accession Number:
      EC 3.1.1.7 (Acetylcholinesterase)
    • Publication Date:
      Date Created: 20000219 Date Completed: 20000404 Latest Revision: 20081121
    • Publication Date:
      20221213
    • Accession Number:
      10.1002/(SICI)1097-0282(200003)53:3<265::AID-BIP6>3.0.CO;2-N
    • Accession Number:
      10679631