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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| Published in | Polymers Vol. 12; no. 2; p. 376 |
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| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
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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. |
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| AbstractList | 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. 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. |
| Author | Stadler, Andreas M Fitter, Jörg Niether, Doreen Wiegand, Simone Sarter, Mona Koenig, Bernd W |
| AuthorAffiliation | 6 Institute of Physical Chemistry, RWTH Aachen University, Landoltweg 2, D-52056 Aachen, Germany 2 I. Physikalisches Institut (IA) & JARA-SOFT, AG Biophysik, RWTH Aachen, Sommerfeldstrasse 14, 52074 Aachen, Germany; mona.sarter@stfc.ac.uk (M.S.); fitter@physik.rwth-aachen.de (J.F.) 7 Department für Chemie—Physikalische Chemie, Universität zu Köln, 50939 Cologne, Germany 3 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; a.stadler@fz-juelich.de 4 Institute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich GmbH, D-52428 Jülich, Germany; b.koenig@fz-juelich.de 1 Institute of Biological Information Processing (IBI-4: Biomacromolecular Systems and Processes) & JARA-SOFT, Forschungszentrum Jülich GmbH, D-52428 Jülich, Germany 5 Institute of Biological Information Processing (IBI-6: Molecular Biophysics), Fors |
| AuthorAffiliation_xml | – name: 6 Institute of Physical Chemistry, RWTH Aachen University, Landoltweg 2, D-52056 Aachen, Germany – name: 1 Institute of Biological Information Processing (IBI-4: Biomacromolecular Systems and Processes) & JARA-SOFT, Forschungszentrum Jülich GmbH, D-52428 Jülich, Germany – name: 5 Institute of Biological Information Processing (IBI-6: Molecular Biophysics), Forschungszentrum Jülich GmbH, D-52428 Jülich, Germany – name: 7 Department für Chemie—Physikalische Chemie, Universität zu Köln, 50939 Cologne, Germany – name: 2 I. Physikalisches Institut (IA) & JARA-SOFT, AG Biophysik, RWTH Aachen, Sommerfeldstrasse 14, 52074 Aachen, Germany; mona.sarter@stfc.ac.uk (M.S.); fitter@physik.rwth-aachen.de (J.F.) – name: 4 Institute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich GmbH, D-52428 Jülich, Germany; b.koenig@fz-juelich.de – name: 3 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; a.stadler@fz-juelich.de |
| Author_xml | – sequence: 1 givenname: Doreen orcidid: 0000-0002-8496-4215 surname: Niether fullname: Niether, Doreen organization: Institute of Biological Information Processing (IBI-4: Biomacromolecular Systems and Processes) & JARA-SOFT, Forschungszentrum Jülich GmbH, D-52428 Jülich, Germany – sequence: 2 givenname: Mona surname: Sarter fullname: Sarter, Mona organization: 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 – sequence: 3 givenname: Bernd W orcidid: 0000-0002-5300-6276 surname: Koenig fullname: Koenig, Bernd W organization: Institute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich GmbH, D-52428 Jülich, Germany – sequence: 4 givenname: Jörg orcidid: 0000-0002-4503-2079 surname: Fitter fullname: Fitter, Jörg organization: Institute of Biological Information Processing (IBI-6: Molecular Biophysics), Forschungszentrum Jülich GmbH, D-52428 Jülich, Germany – sequence: 5 givenname: Andreas M orcidid: 0000-0003-2272-5232 surname: Stadler fullname: Stadler, Andreas M organization: Institute of Physical Chemistry, RWTH Aachen University, Landoltweg 2, D-52056 Aachen, Germany – sequence: 6 givenname: Simone orcidid: 0000-0001-6333-1956 surname: Wiegand fullname: Wiegand, Simone organization: Department für Chemie - Physikalische Chemie, Universität zu Köln, 50939 Cologne, Germany |
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| Keywords | hydrogen bonds thermophoresis protein–ligand binding |
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| Title | Thermophoresis: The Case of Streptavidin and Biotin |
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