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| Home > Publications database > How Hofmeister series influence the thermodiffusion of salts in water? |
| Poster (Other) | FZJ-2021-02180 |
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2021
Please use a persistent id in citations: http://hdl.handle.net/2128/27806
Abstract: Thermal gradients induce a motion of solute molecules towards hot or cold regions. The motion of solutes in a solvent induced by a thermal gradient is termed thermodiffusion. Soret coefficient is used to quantify the ratio of the established concentration gradient to the thermal gradient. This has become an important tool to monitor protein-ligand binding , as it is very sensitive to the nature of solute-water interactions. Buffers, which are used to stabilize the proteins, are multicomponent mixtures with different kinds of salts. Hence to obtain a better understanding of protein-ligand systems, the first step is the investigation of salt solutions. We investigated aqueous solutions of five potassium salts: potassium chloride, potassium bromide, potassium thiocyanate, potassium acetate and potassium carbonate where the corresponding anions cover the full Hofmeister range. We study the thermophoresis of all salt solutions between 15 to 45oC in a molality range between 1 – 5 mol/kg using thermal diffusion forced Rayleigh scattering. We examine, in particular, whether the correlations found for non-ionic solutes are carried over to ionic solutes. Our results are discussed in the context with the ionic and hydrogen bonding contributions to thermophoresis. This study shows how sensitive the thermophoretic phenomenon is to the ion species and its position in the Hofmeister series and how a change of the ion influences thermophoretic properties.
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