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@ARTICLE{Hansen:904359,
      author       = {Hansen, Jan and Uthayakumar, Rajeevann and Pedersen, Jan
                      Skov and Egelhaaf, Stefan U. and Platten, Florian},
      title        = {{I}nteractions in protein solutions close to
                      liquid–liquid phase separation: ethanol reduces
                      attractions via changes of the dielectric solution
                      properties},
      journal      = {Physical chemistry, chemical physics},
      volume       = {23},
      number       = {39},
      issn         = {1463-9076},
      address      = {Cambridge},
      publisher    = {RSC Publ.},
      reportid     = {FZJ-2021-05929},
      pages        = {22384 - 22394},
      year         = {2021},
      abstract     = {Ethanol is a common protein crystallization agent,
                      precipitant, and denaturant, but also alters the dielectric
                      properties of solutions. While ethanol-induced unfolding is
                      largely ascribed to its hydrophobic parts, its effect on
                      protein phase separation and inter-protein interactions
                      remains poorly understood. Here, the effects of ethanol and
                      NaCl on the phase behavior and interactions of protein
                      solutions are studied in terms of the metastable
                      liquid–liquid phase separation (LLPS) and the second
                      virial coefficient B2 using lysozyme solutions.
                      Determination of the phase diagrams shows that the
                      cloud-point temperatures are reduced and raised by the
                      addition of ethanol and salt, respectively. The observed
                      trends can be explained using the extended law of
                      corresponding states as changes of B2. The results for B2
                      agree quantitatively with those of static light scattering
                      and small-angle X-ray scattering experiments. Furthermore,
                      B2 values calculated based on inter-protein interactions
                      described by the Derjaguin-Landau-Verwey-Overbeek (DLVO)
                      potential and considering the dielectric solution properties
                      and electrostatic screening due to the ethanol and salt
                      content quantitatively agree with the experimentally
                      observed B2 values.},
      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       = {pmid:34608908},
      UT           = {WOS:000703642400001},
      doi          = {10.1039/D1CP03210K},
      url          = {https://juser.fz-juelich.de/record/904359},
}