Dynamics of Human Acetylcholinesterase complexed with the covalent Soman inhibitor
Human Acetylcholinesterase (hAChE) is an enzyme, which actually attracts much attention, because it is fundamental for nervous system function being involved in various diseases. In 2009, we measured the dynamics of the sample, complexed or un-complexed with the non-covalent Huperzine A inhibitor as a function of temperature on three different spectrometers (IN6, IN13 and IN16). As result, we found almost no differences in the mean square displacements (MSD’s) of the inhibited enzyme with respect to the native form, but significant variations between both concerning the vibrational density of states (DOS) on IN6 at 80K and QENS measurements taken on IN16. The aim of the present proposal is to repeat the same measurements with hAChE complexed now with the covalent inhibitor Soman, because we are expecting more dramatic effects on the motions in this case. The results will help us to better understand possible relations between enzymatic activities and molecular dynamics.
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PETERS Judith; BEDECARRATS Thomas; BESSET Nicolas; Bernhard Frick; KOZA Michael Marek; MASSON Patrick; NACHON Florian; TEHEI Moeava; TRAPP Marcus; TROVASLET Marie and WEIK Martin. (2012). Dynamics of Human Acetylcholinesterase complexed with the covalent Soman inhibitor. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-04-681
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