% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Hansen:915920,
      author       = {Hansen, Jan and Pedersen, Jannik N. and Pedersen, Jan Skov
                      and Egelhaaf, Stefan U. and Platten, Florian},
      title        = {{U}niversal effective interactions of globular proteins
                      close to liquid–liquid phase separation:
                      {C}orresponding-states behavior reflected in the structure
                      factor},
      journal      = {The journal of chemical physics},
      volume       = {156},
      number       = {24},
      issn         = {0021-9606},
      address      = {Melville, NY},
      publisher    = {American Institute of Physics},
      reportid     = {FZJ-2022-05783},
      pages        = {244903 -},
      year         = {2022},
      abstract     = {Intermolecular interactions in protein solutions, in
                      general, contain many contributions. If short-range
                      attractions dominate, the state diagram exhibits
                      liquid–liquid phase separation (LLPS) that is metastable
                      with respect to crystallization. In this case, the extended
                      law of corresponding states (ELCS) suggests that
                      thermodynamic properties are insensitive to details of the
                      underlying interaction potential. Using lysozyme solutions,
                      we investigate the applicability of the ELCS to the static
                      structure factor and how far effective colloidal interaction
                      models can help to rationalize the phase behavior and
                      interactions of protein solutions in the vicinity of the
                      LLPS binodal. The (effective) structure factor has been
                      determined by small-angle x-ray scattering. It can be
                      described by Baxter’s adhesive hard-sphere model, which
                      implies a single fit parameter from which the normalized
                      second virial coefficient b2 is inferred and found to
                      quantitatively agree with previous results from static light
                      scattering. The b2 values are independent of protein
                      concentration but systematically vary with temperature and
                      solution composition, i.e., salt and additive content. If
                      plotted as a function of temperature normalized by the
                      critical temperature, the values of b2 follow a universal
                      behavior. These findings validate the applicability of the
                      ELCS to globular protein solutions and indicate that the
                      ELCS can also be reflected in the structure factor.},
      cin          = {IBI-4},
      ddc          = {530},
      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       = {35778071},
      UT           = {WOS:000816964600002},
      doi          = {10.1063/5.0088601},
      url          = {https://juser.fz-juelich.de/record/915920},
}