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