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@PHDTHESIS{Niether:858802,
      author       = {Niether, Doreen},
      title        = {{T}hermophoresis of biological and biocompatible systems},
      school       = {Universität zu Köln},
      type         = {Dissertation},
      address      = {Köln},
      reportid     = {FZJ-2018-07642},
      pages        = {160 p.},
      year         = {2018},
      note         = {Dissertation, Universität zu Köln, 2018},
      abstract     = {Thermophoresis, or thermodiffusion, is mass transport
                      driven by a temperature gradient. This work focuses on
                      thermodiffusion in a biological context, where there are two
                      major applications for the effect: accumulation of a
                      component in microfluidic devices through a combination of
                      thermodiffusion and convection, and monitoring of protein
                      binding reactions through the sensitivity of thermodiffusion
                      to complex formation.Both applications are investigated, the
                      first as an accumulation process in the context of
                      origin-of-life theories and the second in light of the
                      question what we can learn from the observed changes in
                      thermodiffusion about modifications of the hydration shell
                      upon complex formation. While thermodiffusion in non-polar
                      liquids can be predicted with reasonable accuracy, the
                      description of aqueous systems is complicated as their
                      concentration and temperature dependence is often anomalous.
                      The underlying goal of this work is to gain a better
                      understanding of the interactions between components in an
                      aqueous mixture and how they influence thermodiffusion.We
                      find that the temperature dependence of a solute's
                      thermodiffusion correlates with its hydrophilicity and argue
                      that the temperature sensitivity of hydrogen bonds, which
                      dominate the interactions in aqueous solutions, might induce
                      a temperature dependence of the chemical potential. Such a
                      temperature dependence is as of yet not considered in
                      theoretical descriptions of thermodiffusion. Numerical
                      calculations show that the thermophoretic accumulation
                      process, as of yet only considered for the formation of RNA,
                      can accumulate formamide to high concentrations that would
                      allow the formation of prebiotic molecules. A heuristic
                      model is developed to illuminate the mechanism behind the
                      accumulation. Cyclodextrins and streptavidin were
                      investigated as model systems for biological complexes. It
                      is feasible that the exquisite sensitivity of
                      thermodiffusion to interactions with the surrounding solvent
                      allows inferences about changes in the protein's hydration
                      shell upon complex formation. Preliminary measurements on
                      streptavidin-biotin show a decreased hydrophilicity of the
                      complex, which is in qualitative agreement with increased
                      entropy of the hydration shell upon complex formation
                      calculated from calorimetric and neutron scattering
                      experiments.},
      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)11},
      url          = {https://juser.fz-juelich.de/record/858802},
}