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Thermophoresis: The Case of Streptavidin and Biotin

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Institute of Biological Information Processing (IBI-4: Biomacromolecular Systems and Processes) & JARA-SOFT, Forschungszentrum Jülich GmbH, D-52428 Jülich, Germany
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I. Physikalisches Institut (IA) & JARA-SOFT, AG Biophysik, RWTH Aachen, Sommerfeldstrasse 14, 52074 Aachen, Germany
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Jülich Centre for Neutron Science (JCNS-1) and Institute of Biological Information Processing (IBI-8: Neutron Scattering and Soft Matter), Forschungszentrum Jülich GmbH, D-52428 Jülich, Germany
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Institute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich GmbH, D-52428 Jülich, Germany
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Institute of Biological Information Processing (IBI-6: Molecular Biophysics), Forschungszentrum Jülich GmbH, D-52428 Jülich, Germany
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Institute of Physical Chemistry, RWTH Aachen University, Landoltweg 2, D-52056 Aachen, Germany
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Department für Chemie - Physikalische Chemie, Universität zu Köln, 50939 Cologne, Germany
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Authors to whom correspondence should be addressed.
Current address: IEK-8, Forschungszentrum Jülich GmbH, D-52428 Jülich, Germany
Current address: ISIS Pulsed Neutron and Muon Facility, Science and Technology FacilitiesCouncil Rutherford Appleton Laboratory, Harwell Science and InnovationCampus, Oxon OX11 0QX, UK
Polymers 2020, 12(2), 376; https://doi.org/10.3390/polym12020376
Received: 11 December 2019 / Revised: 27 January 2020 / Accepted: 29 January 2020 / Published: 7 February 2020
(This article belongs to the Special Issue Synthesis, Characterization and Simulation of Soft Matter with EUSMI)
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.
Keywords: thermophoresis; protein–ligand binding; hydrogen bonds thermophoresis; protein–ligand binding; hydrogen bonds
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MDPI and ACS Style

Niether, D.; Sarter, M.; Koenig, B.W.; Fitter, J.; Stadler, A.M.; Wiegand, S. Thermophoresis: The Case of Streptavidin and Biotin. Polymers 2020, 12, 376.

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