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Intermolecular interactions in protein solutions in general contain manycontributions. If short-range attractions dominate, the state diagram exhibitsliquid-liquid phase separation (LLPS) that is metastable with respect tocrystallization. In this case, the extended law of corresponding states (ELCS)suggests that thermodynamic properties are insensitive to details of theunderlying interaction potential. Using lysozyme solutions, we investigate theapplicability of the ELCS to the static structure factor and in how fareffective colloidal interaction models can help to rationalize the phasebehavior and interactions of protein solutions in the vicinity of the LLPSbinodal. The (effective) structure factor has been determined by small-angleX-ray scattering (SAXS). It can be described by Baxter's adhesive hard-spheremodel, which implies a single fit parameter from which the normalized secondvirial coefficient $b_2$ is inferred and found to quantitatively agree withprevious results from static light scattering. The $b_2$ values are independentof protein concentration, but systematically vary with temperature and solutioncomposition, i.e. salt and additive content. If plotted as a function oftemperature normalized by the critical temperature, the values of $b_2$ followa universal behaviour. These findings validate the applicability of the ELCS toglobular protein solutions and indicate that the ELCS can also be reflected inthe structure factor.

journal of chemical physics online/the journal of chemical physics/journal of chemical physics

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