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

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 asymptot...

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Veröffentlicht in:The Journal of chemical physics 2023-10, Vol.159 (14)
Hauptverfasser: Hassani, Abir N., Haris, Luman, Appel, Markus, Seydel, Tilo, Stadler, Andreas M., Kneller, Gerald R.
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Sprache:eng
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Zusammenfassung: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.
ISSN:0021-9606
1089-7690
DOI:10.1063/5.0166124