title: Electrostatic steering of substrate to acetylcholinesterase: analysis of field fluctuations.
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.
authors.affiliation: National Center for Genome Resources, 1800-A Old Pecos Trail, Santa Fe, NM 87505, USA.
authors.forename: S T
authors.initials: ST
authors.lastname: Wlodek
authors.forename: T
authors.initials: T
authors.lastname: Shen
authors.forename: J A
authors.initials: JA
authors.lastname: McCammon
mesh_terms: D000110:Acetylcholinesterase / Q000737:chemistry*; D004563:Electrochemistry; D020836:Protein Structure, Quaternary; D055672:Static Electricity; D013379:Substrate Specificity
chemical_list: D000110:Acetylcholinesterase