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@ARTICLE{Mohanakumar:911640,
      author       = {Mohanakumar, Shilpa and Lee, Namkyu and Wiegand, Simone},
      title        = {{C}omplementary {E}xperimental {M}ethods to {O}btain
                      {T}hermodynamic {P}arameters of {P}rotein {L}igand
                      {S}ystems},
      journal      = {International journal of molecular sciences},
      volume       = {23},
      number       = {22},
      issn         = {1422-0067},
      address      = {Basel},
      publisher    = {Molecular Diversity Preservation International},
      reportid     = {FZJ-2022-04896},
      pages        = {14198 -},
      year         = {2022},
      abstract     = {In recent years, thermophoresis has emerged as a promising
                      tool for quantifying biomolecular interactions. The
                      underlying microscopic physical effect is still not
                      understood, but often attributed to changes in the hydration
                      layer once the binding occurs. To gain deeper insight, we
                      investigate whether non-equilibrium coefficients can be
                      related to equilibrium properties. Therefore, we compare
                      thermophoretic data measured by thermal diffusion forced
                      Rayleigh scattering (TDFRS) (which is a non-equilibrium
                      process) with thermodynamic data obtained by isothermal
                      titration calorimetry (ITC) (which is an equilibrium
                      process). As a reference system, we studied the chelation
                      reaction between ethylenediaminetetraacetic acid (EDTA) and
                      calcium chloride (CaCl2) to relate the thermophoretic
                      behavior quantified by the Soret coefficient ST to the
                      Gibb’s free energy ΔG determined in the ITC experiment
                      using an expression proposed by Eastman. Finally, we have
                      studied the binding of the protein Bovine Carbonic Anhydrase
                      I (BCA I) to two different benzenesulfonamide derivatives:
                      4-fluorobenzenesulfonamide (4FBS) and
                      pentafluorobenzenesulfonamide (PFBS). For all three systems,
                      we find that the Gibb’s free energies calculated from ST
                      agree with ΔG from the ITC experiment. In addition, we also
                      investigate the influence of fluorescent labeling, which
                      allows measurements in a thermophoretic microfluidic cell.
                      Re-examination of the fluorescently labeled system using ITC
                      showed a strong influence of the dye on the binding
                      behavior.},
      cin          = {IBI-4},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBI-4-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {36430678},
      UT           = {WOS:000887546500001},
      doi          = {10.3390/ijms232214198},
      url          = {https://juser.fz-juelich.de/record/911640},
}