Molecular dynamics of a pair of enantiomers in complex with acetylcholinesterase
The enzyme acetylcholinesterase (AChE) is an essential component of the nervous system, where it catalyses the hydrolysis of the neurotransmitter acetylcholine. In our research, we use this system to investigate fundamental aspects of molecular recognition, mechanism of catalysis/inhibition and rational drug design. In this proposal we would like to investigate the molecular dynamics of AChE in the presence or absence of ligands (inhibitors). After successful investigation of the enzyme with and without inhibitors, it should shed lights on a new aspect newer tested before by neutron scattering. The results obtained by neutron scattering will be related to data from other computational and experimental techniques applied by us to this particular system.
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LINUSSON Anna; ALLGARDSSON Anders; EKSTROM FREDERIK; MARTINEZ Nicolas; PETERS Judith and TROVASLET Marie. (2013). Molecular dynamics of a pair of enantiomers in complex with acetylcholinesterase. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-04-708
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