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Electrostatic steering of substrate to acetylcholinesterase: Analysis of field fluctuations
Author(s) -
Wlodek Stanislaw T.,
Shen Tongye,
McCammon J. Andrew
Publication year - 2000
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/(sici)1097-0282(200003)53:3<265::aid-bip6>3.0.co;2-n
Subject(s) - chemistry , substrate (aquarium) , acetylcholinesterase , molecular dynamics , electrostatics , dimer , field (mathematics) , animation , static electricity , chemical physics , computational chemistry , enzyme , physics , organic chemistry , quantum mechanics , computer graphics (images) , computer science , ecology , mathematics , pure mathematics , biology
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. © 2000 John Wiley & Sons, Inc. Biopoly 53: 265–271, 2000