This title appears in the Scientific Report :
2020
Please use the identifier:
http://dx.doi.org/10.3390/polym12020376 in citations.
Please use the identifier: http://hdl.handle.net/2128/24317 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 / Koenig, Bernd W. / Fitter, Jörg / Stadler, Andreas M. / Wiegand, Simone (Corresponding author) | |
Contributing Institute: |
Molekulare Biophysik; ICS-5 Weiche Materie; ICS-3 Troposphäre; IEK-8 Neutronenstreuung; JCNS-1 Strukturbiochemie; ICS-6 |
Published in: | Polymers, 12 (2020) 2, S. 376 - |
Imprint: |
Basel
MDPI
2020
|
PubMed ID: |
32046223 |
DOI: |
10.3390/polym12020376 |
Document Type: |
Journal Article |
Research Program: |
Tropospheric trace substances and their transformation processes European infrastructure for spectroscopy, scattering and imaging of soft matter Functional Macromolecules and Complexes |
Link: |
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Publikationsportal JuSER |
Please use the identifier: http://hdl.handle.net/2128/24317 in citations.
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. 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). 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. |