Acetylcholinesterase investigated under osmotic pressure
The enzyme acetylcholinesterase (AChE) plays an important role in the nervous system of animals. By rapid hydrolysis of the neurotransmitter acetylcholine, AChE terminates neurotransmission at cholinergic synapses. We already studied the influence of an inhibitor on the dynamics of the enzyme on several spectrometers of the ILL (IN6, IN13 and IN16) [1] and we are currently investigating the effect of high hydrostatic pressure on the dynamics and the structure of this protein [2]. However, up to now all studies were based on the assumption that the solvent was an ideal dilute substance treated as a heat bath. But enzymes found in organisms adapted to very low (psychrophiles) and very high (thermophiles) temperatures are also subjected to variable solute concentrations and viscosities [3]. We now wish to explore the effect of osmotic pressure, which can be obtained by using water-cosolvent mixtures to solvate the protein. This could be very useful for determining the thermodynamics of enzymes catalyzing reactions at temperature extremes in the presence of substrate solutions of different compositions and viscosities.
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PETERS Judith; Bernhard Frick; KOZA Michael Marek; LEME Mathieu; MARION Jeremie; MARTINEZ Nicolas; MASSON Patrick; NACHON Florian; SEYDEL Tilo and TROVASLET Marie. (2013). Acetylcholinesterase investigated under osmotic pressure. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-04-707
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