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@INPROCEEDINGS{Niether:856634,
      author       = {Niether, Doreen and Sarter, Mona and Stadler, Andreas and
                      Wiegand, Simone},
      title        = {{THERMODIFFUSION} {AS} {A} {PROBE} {FOR} {PROTEIN}
                      {HYDRATION}},
      reportid     = {FZJ-2018-05999},
      year         = {2018},
      abstract     = {Protein-ligand interactions are of fundamental importance
                      to numerous processes in living organisms. A very sensitive
                      method to observe the reaction kinetics is Microscale
                      thermophoresis (MST), which uses the changed thermophoretic
                      behaviour as an indicator for complex formation [1]. This
                      sensitivity of thermodiffusion is attributed to
                      modifications in the hydration shell of the protein upon
                      complex formation, which can be strong due to conformational
                      changes of the protein. There is, however, no detailed
                      understanding how protein conformation, hydration and
                      thermophoretic behaviour are connected. Our aim is to
                      elucidate that point and find out if MST could be used to
                      obtain information about protein hydration in addition to
                      the reaction kinetics. Several cyclodextrins and their
                      complexes with acetylsalicylic acid were investigated as a
                      simple model system [2]. We found that the temperature
                      dependence of a solute’s thermodiffusion is correlated to
                      its hydrophilicity, but the observed change upon complex
                      formation is relatively small due to the rigidity of
                      cyclodextrin. The second model system is the protein
                      streptavidin and its complex with biotin [3]. Data from
                      quasi-elastic neutron scattering (QENS) and isothermal
                      titration calorimetry (ITC) show a reduced entropy of the
                      complex in comparison to the free protein, which is partly
                      compensated by an increased entropy of the hydration shell.
                      This is in agreement with a breaking of hydrogen bonds
                      between protein and surrounding water due to the reduced
                      flexibility of the protein [4] and fits with the reduced
                      hydrophilicity of the complex indicated by
                      thermodiffusion.REFERENCES[1] M. Jerabek-Willemsen et al.,
                      J. Mol. Struct. 1077, 101-113 (2014)[2] D. Niether et al.,
                      Langmuir, 33, 8483 (2017).[3] D. Niether et al., AIP
                      Conference Proceedings 1929, 020001 (2018).[4] S. Liese et
                      al., ACS Nano, 11 702 (2017).},
      month         = {Sep},
      date          = {2018-09-11},
      organization  = {13th International Meeting on
                       Thermodiffusion, London (UK), 11 Sep
                       2018 - 14 Sep 2018},
      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/856634},
}