Signature of functional enzyme dynamics in quasielastic neutron scattering spectra: The case of phosphoglycerate kinase.
- Resource Type
- Article
- Authors
- Hassani, Abir N.; Haris, Luman; Appel, Markus; Seydel, Tilo; Stadler, Andreas M.; Kneller, Gerald R.
- Source
- Journal of Chemical Physics. 10/14/2023, Vol. 159 Issue 14, p1-5. 5p.
- Subject
- *PHOSPHOGLYCERATE kinase
*NEUTRON scattering
*QUASI-elastic scattering
*ENZYME kinetics
*ACTIVATION energy
- Language
- ISSN
- 0021-9606
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. [ABSTRACT FROM AUTHOR]