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

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 b...

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Bibliographic Details
Published in:The Journal of chemical physics 2019-04, Vol.150 (16), p.161104-161104
Main Authors: Saouessi, Melek, Peters, Judith, Kneller, Gerald R.
Format: Article
Language:English
Subjects:
Acetylcholinesterase - chemistry
Acetylcholinesterase - metabolism
Binding
Decay rate
Elasticity
Humans
Hydrogen atoms
Ligands
Neutron Diffraction
Neutron scattering
Neutrons
Physics
Protein Binding
Scattering functions
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Summary: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.
ISSN:0021-9606
1089-7690
DOI:10.1063/1.5094625