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Universal effective interactions of globular proteins close to liquid-liquid phase separation: Corresponding-states behavior reflected in the structure factor

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DOI

  • Jan Hansen, Condensed Matter Physics Laboratory, Heinrich Heine University Düsseldorf
  • ,
  • Jannik N. Pedersen
  • ,
  • Jan Skov Pedersen
  • Stefan U. Egelhaaf, Heinrich Heine University Düsseldorf
  • ,
  • Florian Platten, Heinrich Heine University Düsseldorf, Jülich Research Centre

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.

Original languageEnglish
Article number244903
JournalJournal of Chemical Physics
Volume156
Issue24
Number of pages9
ISSN0021-9606
DOIs
Publication statusPublished - Jun 2022

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