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@INPROCEEDINGS{Rudani:1025123,
      author       = {Rudani, Binny and Jakubowski, Andre and Wiegand, Simone},
      title        = {{T}hermodiffusion of {A}queous {S}olutions of {G}uanidinium
                      {S}alts},
      reportid     = {FZJ-2024-02710},
      year         = {2024},
      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.},
      month         = {Mar},
      date          = {2024-03-25},
      organization  = {Bunsen-Tagung 2024, Aachen (Germany),
                       25 Mar 2024 - 27 Mar 2024},
      subtyp        = {Other},
      cin          = {IBI-4},
      cid          = {I:(DE-Juel1)IBI-4-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)24},
      doi          = {10.34734/FZJ-2024-02710},
      url          = {https://juser.fz-juelich.de/record/1025123},
}