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@INPROCEEDINGS{Niether:849923,
      author       = {Niether, Doreen and Sarter, Mona and König, Bernd and
                      Zamponi, Michaela and Fitter, Jörg and Stadler, Andreas and
                      Wiegand, Simone},
      title        = {{T}hermodiffusion as a {P}robe of {P}rotein {L}igand
                      {B}inding},
      reportid     = {FZJ-2018-04019},
      year         = {2018},
      abstract     = {Molecular recognition via protein-ligand interactions is of
                      fundamental importance to numerous processes in living
                      organisms. The behaviour of biomolecules in a temperature
                      gradient, known as thermodiffusion or thermophoresis,
                      changes when a ligand binds. Microscale thermophoresis (MST)
                      uses this sensitivity of the thermophoretic response to
                      access information on binding dynamics, although the
                      physicochemical processes are still unclear [1].
                      Additionally, thermophoresis is promising as a tool to gain
                      information on the hydration layer and how it changes due to
                      complex formation. We use infra-red thermal diffusion forced
                      Rayleigh scattering (IR-TDFRS) in a temperature range from
                      10 to 50°C to investigate the thermodiffusion properties.
                      In previous studies [2] we used cyclodextrin-aspirin as a
                      model system for complexes and showed that the temperature
                      dependence of the thermodiffusion behaviour is sensitive to
                      solute-solvent interactions. Now we shift our focus to the
                      protein streptavidin (SA) and its biotin complex. Similar to
                      the cyclodextrins, formation of the SA-biotin complex leads
                      to a weaker temperature sensitivity of the thermodiffusion
                      behaviour, although the effect is more pronounced. This
                      indicates a less hydrophilic complex. To quantify the
                      influence of structural fluctuations and conformational
                      motion of the protein on the entropy change of its hydration
                      layer upon ligand binding, we combine quasi-elastic
                      incoherent neutron scattering (QENS) and isothermal
                      titration calorimetry (ITC) data. As the QENS measurements
                      are only possible in heavy water, the ITC need to be
                      performed in heavy water as well in order to gain a better
                      understanding of the hydration layer. The aim of this work
                      is to develop a microscopic understanding of the correlation
                      between the strength of solute-solvent interactions and the
                      thermophoretic behaviour.[1] M. Jerabek-Willemsen et al., J.
                      Mol. Struct. (2014).[2] D. Niether et al., Langmuir 33(34),
                      8483-8492 (2017).},
      month         = {Jun},
      date          = {2018-06-24},
      organization  = {Twentieth Symposium on Thermophysical
                       Properties, Boulder (USA), 24 Jun 2018
                       - 29 Jun 2018},
      subtyp        = {Invited},
      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/849923},
}