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@INPROCEEDINGS{Niether:849925,
      author       = {Niether, Doreen and Di Lecce, Silvia and Bresme, Fernando
                      and Wiegand, Simone},
      title        = {{U}nravelling the hydrophobicity of urea in water using
                      thermodiffusion: implications for protein denaturation},
      reportid     = {FZJ-2018-04021},
      year         = {2018},
      abstract     = {Urea is widely used as protein denaturant in aqueous
                      solutions. Experiments and computer simulation studies have
                      shown that it dissolves in water almost ideally at high
                      concentrations, introducing little disruption in the water
                      hydrogen bonded structure. However, at concentrations of the
                      order of 5 M or higher, urea induces denaturation in a wide
                      range of proteins. The origin of this behaviour is not
                      completely understood, but it is believed to stem from a
                      balance between urea-protein and urea-water interactions,
                      with urea becoming possibly hydrophobic at a specific
                      concentration range. The small changes observed in the water
                      structure makes it difficult to connect the denaturation
                      effects to solvation properties. Here we show that the
                      exquisite sensitivity of thermodiffusion to solute-water
                      interactions allows the identification of the onset of
                      hydrophobicity of urea-water mixtures. The hydrophobic
                      behaviour is reflected in a sign reversal of the temperature
                      dependent slope of the Soret coefficient, which is observed,
                      both in experiments and non-equilibrium computer simulations
                      at approximately 5 M concentration of urea in water. This
                      concentration regime corresponds to the one where abrupt
                      changes in the denaturation of proteins are commonly
                      observed. We show that the onset of hydrophobicity is
                      intrinsically connected to the urea-water interactions. Our
                      results allow us to identify correlations between the Soret
                      coefficient and the partition coefficient, logP, hence
                      establishing the thermodiffusion technique as a powerful
                      approach to study hydrophobicity.},
      month         = {Jun},
      date          = {2018-06-24},
      organization  = {Twentieth Symposium on Thermophysical
                       Properties, Boulder (USA), 24 Jun 2018
                       - 29 Jun 2018},
      subtyp        = {After Call},
      cin          = {ICS-3},
      cid          = {I:(DE-Juel1)ICS-3-20110106},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)6},
      url          = {https://juser.fz-juelich.de/record/849925},
}