Electrostatic steering of substrate to acetylcholinesterase: analysis of field fluctuations

Biopolymers. 2000 Mar;53(3):265-71. doi: 10.1002/(SICI)1097-0282(200003)53:3<265::AID-BIP6>3.0.CO;2-N.

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.

Publication types

  • 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.

MeSH terms

  • Acetylcholinesterase / chemistry*
  • Electrochemistry
  • Protein Structure, Quaternary
  • Static Electricity
  • Substrate Specificity

Substances

  • Acetylcholinesterase