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@ARTICLE{Niether:858228,
      author       = {Niether, Doreen and Kriegs, Hartmut and Dhont, Jan K. G.
                      and Wiegand, Simone},
      title        = {{P}eptide model systems: {C}orrelation between
                      thermophilicity and hydrophilicity},
      journal      = {The journal of chemical physics},
      volume       = {149},
      number       = {4},
      issn         = {1089-7690},
      address      = {Melville, NY},
      publisher    = {American Institute of Physics},
      reportid     = {FZJ-2018-07128},
      pages        = {044506 -},
      year         = {2018},
      abstract     = {In recent years, the response of biomolecules to a
                      temperature gradient has been utilized to monitor reactions
                      of biomolecules, but the underlying mechanism is not well
                      understood due to the complexity of the multicomponent
                      system. To identify some underlying principles, we
                      investigate the thermal diffusion of small amide molecules
                      in water systematically. We re-analyze previous measurements
                      of urea and formamide and compare the results with
                      acetamide, N-methylformamide, and N, N-dimethylformamide,
                      amides with a lower hydrophilicity. It turns out that less
                      hydrophilic substances do not show the typical temperature
                      dependence of water soluble macromolecules. Analyzing
                      temperature and concentration dependent measurements using
                      an empirical expression originally derived for nonpolar
                      mixtures, we find that the so-called isotope contribution
                      depends strongly on the hydrophilicity of the solute. This
                      can be qualitatively understood by comparing with molecular
                      dynamic simulations of Lennard-Jones fluids. The
                      hydrophobic/hydrophilic balance also influences the
                      structure in the fluid and with that the thermal expansion
                      coefficient, which correlates with the thermal diffusion
                      coefficient. Furthermore, we observe a clear correlation of
                      the temperature and concentration dependence of the Soret
                      coefficient with the hydrophilicity, which can be
                      quantitatively described by the partition coefficient log P},
      cin          = {ICS-3},
      ddc          = {530},
      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)16},
      pubmed       = {pmid:30068171},
      UT           = {WOS:000440586200041},
      doi          = {10.1063/1.5042051},
      url          = {https://juser.fz-juelich.de/record/858228},
}