Abstract
We determine the phase diagrams of two widely studied protein solutions, namely, lysozyme and γ-crystallin in water and added salt, within a short-range, pair-potential representation of macroparticle interactions. A one-parameter fit of the model is performed on the basis of static or dynamic light scattering and self-interaction chromatography data. Demixing and crystallization curves, as calculated through numerical approaches, turn out to be in good agreement with experimental protein-rich−protein-poor and solubility envelopes. Our findings highlight the minimal assumptions about the nature of the microscopic potential allowing a satisfactory reproduction of the phase-diagram topology of globular protein solutions.
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