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@INPROCEEDINGS{Niether:818394,
      author       = {Niether, Doreen and Dhont, Jan K.G. and Wiegand, Simone},
      title        = {{H}ow do hydrogen bonds influence thermophoresis?},
      reportid     = {FZJ-2016-04855},
      year         = {2016},
      abstract     = {So far there is only a limited microscopic understanding of
                      thermodiffusion for fluids. Especially inaqueous systems the
                      situation is complicated due to charge effects and strong
                      specific crossinteractions. On the other hand a detailed
                      understanding of aqueous systems would be valuable due
                      toimportant applications in biotechnology, where the
                      response to temperature gradients is successfullyemployed to
                      monitor reaction kinetics of large proteins with small
                      ligand molecules [1]. The strongsensitivity of proteins and
                      other water soluble biomolecules is probably caused by a
                      change in thehydration layer, which is influenced by subtle
                      conformation changes induced by the binding of theligand
                      molecule. One key parameter is the understanding of hydrogen
                      bonds in the thermophoreticprocess [2]. To gain a better
                      understanding of underlying physical process we
                      systematicallyinvestigated various hydrogen bond formers
                      (urea, acetamide, formamide, methylformamide) in waterby a
                      holographic grating method called infrared thermal diffusion
                      forced Rayleigh scattering (IRTDFRS).We elucidate the often
                      found typical temperature dependence of the Soret
                      coefficient ofsolute molecules in water and claim that this
                      simple empirical approach to describe the
                      temperaturedependence breaks down at higher solute
                      concentrations, when interactions between different
                      solutemolecules start to play a role. Additionally the
                      concept also requires a hydrogen bond network
                      withoutmicro-heterogeneities or cage structures. For
                      nucleotides we found a correlation between the
                      partitioncoefficient logP and the measured Soret coefficient
                      [3]. As the logP parameter is one of the propertieswhich is
                      included in the so called Lipinski's rule of five for
                      selecting drug compounds, we check thiscorrelation for a
                      number of simple heterocyclic compounds (pyridine, diazines,
                      triazine). Thesenitrogen heterocycles, especially
                      pyrimidine, are partial structures found in many
                      biologically relevantsubstances such as nucleobases,
                      vitamins, alcaloids and drugs (e.g. barbiturates and
                      antibiotics).[1] M. Jerabek-Willemsen, T. André, W. Wanner
                      et al., J. Mol. Struct., 1077, 101 (2014).[2] K. Maeda, N.
                      Shinyashiki, S. Yagihara et al., J. Chem. Phys., 143, 124504
                      (2015).[3] Z. Wang, H. Kriegs and S. Wiegand, J. Phys. Chem.
                      B, 116, 7463 (2012).},
      month         = {Sep},
      date          = {2016-09-12},
      organization  = {4th International Soft Matter
                       Conference, Grenoble (France), 12 Sep
                       2016 - 16 Sep 2016},
      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/818394},
}