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Article Dans Une Revue Journal of Chemical Physics Année : 2023

Signature of functional enzyme dynamics in quasielastic neutron scattering spectra: The case of phosphoglycerate kinase

Abir Hassani
Luman Haris
Markus Appel
Tilo Seydel
Andreas Stadler
Gerald Kneller

Résumé

We present an analysis of high-resolution quasi-elastic neutron scattering spectra of phosphoglycerate kinase which elucidates the influence of the enzymatic activity on the dynamics of the protein. We show that in the active state the inter-domain motions are amplified and the intra-domain asymptotic power-law relaxation ∝t−α is accelerated, with a reduced coefficient α. Employing an energy landscape picture of protein dynamics, this observation can be translated into a widening of the distribution of energy barriers separating conformational substates of the protein.

Dates et versions

hal-04383690 , version 1 (09-01-2024)

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Abir Hassani, Luman Haris, Markus Appel, Tilo Seydel, Andreas Stadler, et al.. Signature of functional enzyme dynamics in quasielastic neutron scattering spectra: The case of phosphoglycerate kinase. Journal of Chemical Physics, 2023, 159 (14), ⟨10.1063/5.0166124⟩. ⟨hal-04383690⟩
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