Journal Article FZJ-2020-00655

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Thermophoresis: The Case of Streptavidin and Biotin

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2020
MDPI Basel

Polymers 12(2), 376 - () [10.3390/polym12020376]

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Abstract: 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.

Classification:

Contributing Institute(s):
  1. Troposphäre (IEK-8)
  2. Weiche Materie (ICS-3)
  3. Molekulare Biophysik (ICS-5)
  4. Strukturbiochemie (ICS-6)
  5. Neutronenstreuung (JCNS-1)
Research Program(s):
  1. 551 - Functional Macromolecules and Complexes (POF3-551) (POF3-551)
  2. EUSMI - European infrastructure for spectroscopy, scattering and imaging of soft matteer (731019) (731019)
  3. 243 - Tropospheric trace substances and their transformation processes (POF3-243) (POF3-243)

Appears in the scientific report 2020
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Medline ; Creative Commons Attribution CC BY 4.0 ; DOAJ ; OpenAccess ; Clarivate Analytics Master Journal List ; Current Contents - Physical, Chemical and Earth Sciences ; DOAJ Seal ; Ebsco Academic Search ; IF < 5 ; JCR ; SCOPUS ; Science Citation Index Expanded ; Web of Science Core Collection
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Document types > Articles > Journal Article
Institute Collections > ER-C > ER-C-3
Institute Collections > JCNS > JCNS-1
Institute Collections > IBI > IBI-6
Institute Collections > IBI > IBI-7
Institute Collections > ICE > ICE-3
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Workflow collections > Publication Charges
ICS > ICS-3
ICS > ICS-5
IEK > IEK-8
ICS > ICS-6
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Open Access

 Record created 2020-01-29, last modified 2024-07-12