Effect of red blood cell shape changes on haemoglobin interactions and dynamics : A neutron scattering study: Hb Interactions and Dynamics in RBCs
(2020) In Royal Society Open Science 7(10).- Abstract
By using a combination of experimental neutron scattering techniques, it is possible to obtain a statistical perspective on red blood cell (RBC) shape in suspensions, and the inter-relationship with protein interactions and dynamics inside the confinement of the cell membrane. In this study, we examined the ultrastructure of RBC and protein-protein interactions of haemoglobin (Hb) in them using ultra-small-angle neutron scattering and small-angle neutron scattering (SANS). In addition, we used the neutron backscattering method to access Hb motion on the ns time scale and Å length scale. Quasi-elastic neutron scattering (QENS) experiments were performed to measure diffusive motion of Hb in RBCs and in an RBC lysate. By using QENS, we... (More)
By using a combination of experimental neutron scattering techniques, it is possible to obtain a statistical perspective on red blood cell (RBC) shape in suspensions, and the inter-relationship with protein interactions and dynamics inside the confinement of the cell membrane. In this study, we examined the ultrastructure of RBC and protein-protein interactions of haemoglobin (Hb) in them using ultra-small-angle neutron scattering and small-angle neutron scattering (SANS). In addition, we used the neutron backscattering method to access Hb motion on the ns time scale and Å length scale. Quasi-elastic neutron scattering (QENS) experiments were performed to measure diffusive motion of Hb in RBCs and in an RBC lysate. By using QENS, we probed both internal Hb dynamics and global protein diffusion, on the accessible time scale and length scale by QENS. Shape changes of RBCs and variation of intracellular Hb concentration were induced by addition of the Na + -selective ionophore monensin and the K + -selective one, valinomycin. The experimental SANS and QENS results are discussed within the framework of crowded protein solutions, where free motion of Hb is obstructed by mutual interactions.
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- author
- Shou, Keyun ; Sarter, Mona ; De Souza, Nicolas R. ; De Campo, Liliana ; Whitten, Andrew E. ; Kuchel, Philip W. ; Garvey, Christopher J. LU and Stadler, Andreas M.
- organization
- publishing date
- 2020
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- haemoglobin, protein diffusion, protein interactions, quasi-elastic neutron scattering, red blood cells, small-angle neutron scattering
- in
- Royal Society Open Science
- volume
- 7
- issue
- 10
- article number
- 201507
- publisher
- Royal Society Publishing
- external identifiers
-
- scopus:85096304647
- ISSN
- 2054-5703
- DOI
- 10.1098/rsos.201507rsos201507
- language
- English
- LU publication?
- yes
- id
- 019a69a5-1698-43df-ba5f-5178ecd6a6f2
- date added to LUP
- 2020-12-02 07:13:47
- date last changed
- 2022-11-16 03:24:04
@article{019a69a5-1698-43df-ba5f-5178ecd6a6f2, abstract = {{<p>By using a combination of experimental neutron scattering techniques, it is possible to obtain a statistical perspective on red blood cell (RBC) shape in suspensions, and the inter-relationship with protein interactions and dynamics inside the confinement of the cell membrane. In this study, we examined the ultrastructure of RBC and protein-protein interactions of haemoglobin (Hb) in them using ultra-small-angle neutron scattering and small-angle neutron scattering (SANS). In addition, we used the neutron backscattering method to access Hb motion on the ns time scale and Å length scale. Quasi-elastic neutron scattering (QENS) experiments were performed to measure diffusive motion of Hb in RBCs and in an RBC lysate. By using QENS, we probed both internal Hb dynamics and global protein diffusion, on the accessible time scale and length scale by QENS. Shape changes of RBCs and variation of intracellular Hb concentration were induced by addition of the Na + -selective ionophore monensin and the K + -selective one, valinomycin. The experimental SANS and QENS results are discussed within the framework of crowded protein solutions, where free motion of Hb is obstructed by mutual interactions.</p>}}, author = {{Shou, Keyun and Sarter, Mona and De Souza, Nicolas R. and De Campo, Liliana and Whitten, Andrew E. and Kuchel, Philip W. and Garvey, Christopher J. and Stadler, Andreas M.}}, issn = {{2054-5703}}, keywords = {{haemoglobin; protein diffusion; protein interactions; quasi-elastic neutron scattering; red blood cells; small-angle neutron scattering}}, language = {{eng}}, number = {{10}}, publisher = {{Royal Society Publishing}}, series = {{Royal Society Open Science}}, title = {{Effect of red blood cell shape changes on haemoglobin interactions and dynamics : A neutron scattering study: Hb Interactions and Dynamics in RBCs}}, url = {{http://dx.doi.org/10.1098/rsos.201507rsos201507}}, doi = {{10.1098/rsos.201507rsos201507}}, volume = {{7}}, year = {{2020}}, }