This title appears in the Scientific Report :
2020
Please use the identifier:
http://hdl.handle.net/2128/26544 in citations.
Thermophoresis: The Case of Streptavidin and Biotin
Thermophoresis: The Case of Streptavidin and Biotin
Thermophoretic behavior of a free protein changes upon ligand binding and gives access to information on the binding constants. The Soret effect has also been proven to be a promising tool to gain information on the hydration layer, as the temperature dependence of the thermodiffusion behavior is se...
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Personal Name(s): | Niether, Doreen (Corresponding author) |
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Sarter, Mona / König, Bernd / Fitter, Jörg / Stadler, Andreas / Wiegand, Simone | |
Contributing Institute: |
Troposphäre; IEK-8 Biomakromolekulare Systeme und Prozesse; IBI-4 |
Imprint: |
2020
|
Conference: | 2020 EUSMI User Meeting, virtual conference (Germany), 2020-11-19 - 2020-11-19 |
Document Type: |
Conference Presentation |
Research Program: |
Functional Macromolecules and Complexes |
Link: |
OpenAccess |
Publikationsportal JuSER |
Thermophoretic behavior of a free protein changes upon ligand binding and gives access to information on the binding constants. The Soret effect has also been proven to be a promising tool to gain information on the hydration layer, as the temperature dependence of the thermodiffusion behavior is sensitive to solute-solvent interactions [1]. In this work, we perform systematic thermophoretic measurements of the protein streptavidin (STV) and of the complex STV with biotin (B) using thermal diffusion forced Rayleigh scattering (TDFRS) [2]. Our experiments show that the temperature sensitivity of the Soret coefficient is reduced for the complex compared to the free protein. We discuss our data in comparison with recent quasi-elastic neutron scattering (QENS) measurements. As the QENS measurement has been performed in heavy water, we perform additional measurements in water/heavy water mixtures. Finally, we also elucidate the challenges arising from the quantiative thermophoretic study of complex multicomponent systems such as protein solutions. References[1] “Thermophoresis of biological and biocompatible compounds in aqueous solution”; Niether, D; Wiegand, S.; J. Phys. Condens. Matter, 31, 503003, (2019). DOI: 10.1088/1361-648X/ab421c[2] “Thermophoresis: The Case of Streptavidin and Biotin”; Niether, D; Sarter, M; Koenig, B.W. et al; Polymers, 12, 376, (2020). DOI: 10.3390/polym12020376. |