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Updated: Jan 25, 2026

Contrast-Matching Detergent in Small-Angle Neutron Scattering Experiments for Membrane Protein Structural Analysis and Ab Initio Modeling
Published on: October 21, 2018
Asymptotic analysis of quasielastic neutron scattering data from human acetylcholinesterase reveals subtle dynamical
Melek Saouessi1, Judith Peters2, Gerald R Kneller1
1Centre de Biophysique Moléculaire, CNRS and Université d'Orléans, Rue Charles Sadron, 45071 Orléans, France.
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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