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• W2088508714 endingPage "7205" @default.
• W2088508714 startingPage "7197" @default.
• W2088508714 abstract "A molecular-thermodynamic analysis of protein partitioning in an aqueous two-phase system shows that the partition coefficient for a native (globular) protein is very much different from that for a denatured (linear) protein; while the former is weakly dependent on protein molecular weight, the latter depends strongly on molecular weight. The native protein and the denatured protein are represented, respectively, by a spherical macroion and by a linear flexible polyion. On the basis of McMillan−Mayer solution theory, the interactions between particles are represented by a continuum-averaged potential of mean force containing hard-sphere repulsion, the effect of penetration or hydration forces, electrostatic interactions, osmotic attraction, and specific interactions. Phase diagrams are calculated for polymer−polymer and for polymer−salt aqueous two-phase-forming systems in good agreement with experiment. Coupled with measured data for obtaining model parameters, partition coefficients are calculated for a native protein, lysozyme. Calculated partition coefficients for a denatured protein are compared with experimental partitioning data for short peptides. Calculated results are remarkably similar to those observed." @default.
• W2088508714 created "2016-06-24" @default.
• W2088508714 creator A5020540558 @default.
• W2088508714 creator A5060450036 @default.
• W2088508714 date "2000-07-27" @default.
• W2088508714 modified "2023-10-09" @default.
• W2088508714 title "Molecular Thermodynamics for Partitioning of Native and Denatured Proteins in Aqueous Two-Phase Systems" @default.
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• W2088508714 doi "https://doi.org/10.1021/jp994371h" @default.
• W2088508714 hasPublicationYear "2000" @default.
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