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| Poster (Other) | FZJ-2024-02710 |
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2024
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Please use a persistent id in citations: doi:10.34734/FZJ-2024-02710
Abstract: Thermodiffusion, or the Ludwig-Soret effect, refers to the motion of solute molecules induced by a thermal gradient. This phenomenon is quantified by the Soret coefficient (ST), in aqueous solutions ST is highly sensitive to the nature of solute-water interactions. It is being used as a tool to probe molecular interactions, mainly protein-ligand binding. Guanidinium ions play a pivotal role in the exploration of protein folding, denaturation, and the hydration of biological molecules owing to its rigid and symmetric structure. Despite its significance, there is a dearth of information on their thermophoretic behaviour. Recent research by our group has delved into the thermodiffusion of similar non-ionic organic solutes and simple ionic inorganic salts in aqueous solutions, revealing distinctive temperature and concentration dependencies of the ST. In our present research, we utilize thermal diffusion forced Rayleigh scattering (TDFRS) to scrutinize guanidinium salt solution with various anions (carbonate, chloride, iodide and thiocyanate), spanning the entire range of the Hofmeister series from hydrophilic to hydrophobic. We performed systematic measurements of ST in a temperature range of 15 to 35°C and concentrations ranging from 0.5m to 3 m. The change of ST withtemperature as a function of increasing concentration becomes weaker for aqueous guanidinium salt solutions. We assume that fewer hydrogen bonds are present at higher concentrations reducing the change of the Soret coefficient and indicatingthat the hydration of the salt plays an important role. Overall, this systematic study helps to gain a fundamental understanding of thermodiffusion in protein-ligand systems.
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