作者: Giuseppe Pellicane , Dino Costa , Carlo Caccamo
DOI: 10.1021/JP048651V
关键词: Lysozyme 、 Globular protein 、 Thermodynamics 、 Analytical chemistry 、 Topology (chemistry) 、 Dynamic light scattering 、 Chemistry 、 Solubility 、 Crystallin 、 Phase diagram 、 Crystallization
摘要: We determine the phase diagrams of two widely studied protein solutions, namely, lysozyme and γ-crystallin in water added salt, within a short-range, pair-potential representation macroparticle interactions. A one-parameter fit model is performed on basis static or dynamic light scattering self-interaction chromatography data. Demixing crystallization curves, as calculated through numerical approaches, turn out to be good agreement with experimental protein-rich−protein-poor solubility envelopes. Our findings highlight minimal assumptions about nature microscopic potential allowing satisfactory reproduction phase-diagram topology globular solutions.