Determination of productive conformations of acetylcholinesterase substrates using theoretical conformational analysis.

All equilibrium conformations of twenty-three acetylcholinesterase effectors were calculated by the molecular mechanics method, nonbonded interactions, torsion energy and energy of bond angles deformation being taken into account. In a series of conformationally flexible derivatives of acetylcholine the correlation was found between hydrolysis rate and population of the completely extended tt-conformation. In a series of cyclic analogues of …