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@INPROCEEDINGS{Bjelcic:858980,
      author       = {Bjelcic, Monika and Niether, Doreen and Dhont, Jan K.G. and
                      Wiegand, Simone},
      title        = {{U}nderstanding {M}icroscale {T}hermophoresis:
                      contributions by simple building blocks of proteins},
      reportid     = {FZJ-2018-07806},
      year         = {2018},
      abstract     = {Understanding Microscale Thermophoresis:Contributions by
                      simple building blocks of proteinsM.Bjelcic, D. Niether1 and
                      S.Wiegand1;21ICS-3 Soft Condensed Matter, Forschungszentrum
                      Jülich GmbH, D-52428 Jülich, Germany2Department für
                      Chemie - Physikalische Chemie, Universität zu Köln, 50939
                      Cologne,GermanyE-mail: s.wiegand@fz-juelich.deIn recent
                      years Microscale Thermophoresis (MST), an analytical
                      approach to monitor proteinligandbinding reactions, gained a
                      lot of interest [1]. This method needs less sample
                      comparedto calorimetric methods and is therefore very useful
                      for pharmaceutical applications. Even forsimple molecules
                      the underlying microscopic processes are not understood. The
                      situation iseven more complicated in the case of proteins.
                      Depending on their folding state they behaveas charged rigid
                      colloids or more flexible polymers. When conformational
                      changes modify theratio of hydrophilic and hydrophobic side
                      groups in contact with water, this influences the
                      hydrationlayer. There is a superb sensitivity of the
                      thermophoretic behaviour of the protein due tothese local
                      rearrangements of water molecules. Recent experiments for
                      various amides showeda clear correlation of the temperature
                      dependence of the Soret coefficient with the
                      hydrophilicity[2], quantitatively described by the logarithm
                      of the 1-octanol/water partition coefficient P.This
                      coefficient is a measure for the
                      hydrophilicity/hydrophobicity balance of a solute and
                      isoften used to model the transport of a compound in the
                      environment or to screen for potentialpharmaceutical
                      compounds. It could be shown that the concept works also for
                      sugars, nonsteroidalanti-inflammatory drugs and
                      cyclodextrins [3]. As it is known that also the ionic
                      strengthand charges have a strong influence on the observed
                      thermophoretic behavior [4], we investigatesystematically
                      various aqueous solutions of alcohols and amino acids with
                      varying hydrophobicity,polarity and charge of the side
                      groups. As experimental method we use a holographicgrating
                      technique called infrared Thermal Diffusion Forced Rayleigh
                      Scattering (IR-TDFRS).References[1] M. Jerabek-Willemsen, T.
                      Andre, R. Wanner, H. M. Roth, S. Duhr, P. Baaske and
                      D.Breitsprecher, J. Mol. Struct., 1077, 101-113, (2014)[2]
                      D. Niether, H. Kriegs, J. K. G. Dhont and S.Wiegand, J.
                      Chem. Phy., (2018) under review[3] D. Niether, T. Kawaguchi,
                      J. Hovancova, K. Eguchi, J. K. G. Dhont, R. Kita and S.
                      Wiegand,Langmuir 33, 8483-8492, (2017)[4] H. Ning, J. K. G.
                      Dhont and S. Wiegand, Langmuir, 24, 2426-2432, (2008)},
      month         = {Nov},
      date          = {2018-11-20},
      organization  = {Jülich Soft Matter Days, Jülich
                       (Germany), 20 Nov 2018 - 23 Nov 2018},
      subtyp        = {Other},
      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)24},
      url          = {https://juser.fz-juelich.de/record/858980},
}