Asymptotic analysis of quasielastic neutron scattering data from human acetylcholinesterase reveals subtle dynamical changes upon ligand binding

Abstract : In this paper, we show that subtle changes in the internal dynamics of human acetylcholinesterase upon ligand binding can be extracted from quasielastic neutron scattering data by employing a nonexponential relaxation model for the intermediate scattering function. The relaxation is here described by a stretched Mittag-Leffler function, which exhibits slow power law decay for long times. Our analysis reveals that binding of a Huperzine A ligand increases the atomic motional amplitudes of the enzyme and slightly slows down its internal diffusive motions. This result is interpreted within an energy landscape picture for the motion of the hydrogen atoms.
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Submitted on : Friday, June 14, 2019 - 3:14:22 PM
Last modification on : Sunday, June 16, 2019 - 1:03:15 AM

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Melek Saouessi, Judith Peters, Gerald Kneller. Asymptotic analysis of quasielastic neutron scattering data from human acetylcholinesterase reveals subtle dynamical changes upon ligand binding. Journal of Chemical Physics, American Institute of Physics, 2019, 150 (16), pp.161104. ⟨10.1063/1.5094625⟩. ⟨hal-02156638⟩

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