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@INPROCEEDINGS{Wiegand:835134,
      author       = {Wiegand, Simone},
      title        = {{W}hat can we learn about complex formation by combining
                      thermophoresis with {QENS}?},
      school       = {TUM},
      reportid     = {FZJ-2017-05002},
      year         = {2017},
      abstract     = {Molecular recognition via protein–ligand interactions is
                      of fundamental importance to most processes occurring within
                      living organisms. Structural fluctuations and conformational
                      motions of proteins are essential for the binding of ligands
                      and other interaction partners. This binding process is
                      governed by equilibrium thermodynamics and the minimization
                      of the free energy ΔG for the whole system. Also the
                      thermophoresis, the diffusion in a temperature gradient, is
                      sensitive to the complex formation. This effect has been
                      used intensively to gain detailed information on binding
                      dynamics, but the physicochemical processes are still
                      unclear [1]. The strong sensitivity of proteins and other
                      water soluble biomolecules to the temperature gradient is
                      probably caused by a change in the hydration layer, which is
                      influenced by subtle conformation changes induced by the
                      binding of the ligand molecule. We want to correlate the
                      information about the hydration layer obtained in
                      thermophoresis experiments with changes of structural
                      fluctuations and conformational motions measured by
                      quasi-elastic incoherent neutron scattering (QENS) and
                      isothermal titration calorimetry (ITC). As model system we
                      want to study streptavidin-biotin. Streptavidin is a 58.8
                      kDa protein with an extremely high affinity for the ligand
                      biotin (also known as vitamin B7 or vitamin H). The
                      thermodiffusion is investigated by infrared thermal
                      diffusion forced Rayleigh scattering (IR-TDFRS) [2]. [1] M.
                      Jerabek-Willemsen, T. André, W. Wanner, H. M. Roth, S.
                      Duhr, P. Baaske, D. Breitsprecher, J. Mol. Struct. 2014,
                      1077, 101-113.[2] S. Wiegand, H. Ning, H. Kriegs, J. Phys.
                      Chem. B 2007, 111, 14169-14174.},
      organization  = {Garching (Germany)},
      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)31},
      url          = {https://juser.fz-juelich.de/record/835134},
}