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000873342 1001_ $$0P:(DE-Juel1)166572$$aNiether, Doreen$$b0$$eCorresponding author
000873342 245__ $$aThermophoresis: The Case of Streptavidin and Biotin
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000873342 520__ $$aThermophoretic 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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000873342 7001_ $$0P:(DE-Juel1)171618$$aSarter, Mona$$b1
000873342 7001_ $$0P:(DE-Juel1)132009$$aKoenig, Bernd W.$$b2
000873342 7001_ $$0P:(DE-Juel1)131961$$aFitter, Jörg$$b3
000873342 7001_ $$0P:(DE-Juel1)140278$$aStadler, Andreas M.$$b4
000873342 7001_ $$0P:(DE-Juel1)131034$$aWiegand, Simone$$b5$$eCorresponding author
000873342 773__ $$0PERI:(DE-600)2527146-5$$a10.3390/polym12020376$$gVol. 12, no. 2, p. 376 -$$n2$$p376 -$$tPolymers$$v12$$x2073-4360$$y2020
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