Frequency domain modeling of quasielastic neutron scattering from hydrated protein powders: Application to free and inhibited human acetylcholinesterase - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Journal of Chemical Physics Année : 2019

Frequency domain modeling of quasielastic neutron scattering from hydrated protein powders: Application to free and inhibited human acetylcholinesterase

Résumé

This article reports on a frequency domain analysis of quasielastic neutron scattering spectra from free and Huperzine-A-inhibited human acetylcholinesterase, extending a recent time domain analysis of the same experimental data [M. Saouessi et al., J. Chem. Phys. 150, 161104 (2019)]. An important technical point here is the construction of a semianalytical model for the resolution-broadened dynamic structure factor that can be fitted to the experimental spectra. We find comparable parameters as in our previous study and demonstrate that our model is sensitive to subpercent changes in the experimental data, which are caused by reversible binding of the inhibitor Huperzine A.
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Dates et versions

hal-02394152 , version 1 (04-12-2019)

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Melek Saouessi, Judith Peters, Gérald Kneller. Frequency domain modeling of quasielastic neutron scattering from hydrated protein powders: Application to free and inhibited human acetylcholinesterase. Journal of Chemical Physics, 2019, 151 (12), pp.125103. ⟨10.1063/1.5121703⟩. ⟨hal-02394152⟩
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