Publication | Closed Access
Liquid‐liquid phase separations in aqueous solutions of globular proteins
58
Citations
33
References
1993
Year
Protein ChemistryObserved Solubility BehaviorEngineeringProtein FoldingMedicineBiopolymersMolecular SimulationProtein Phase SeparationPhase SeparationAnalytical UltracentrifugationGlobular ProteinsLiquid‐liquid Phase SeparationsBiophysicsBiomolecular EngineeringProtein Purification
Abstract A simple statistical‐mechanical theory, known as the random‐phase approximation, is applied to study liquid‐liquid phase separations in solutions of globular proteins. Phase separation may be induced by addition of nonionic polymer or/and ordinary electrolytes. In this analysis, the osmotic‐attraction mechanism, whereby the depletion of “solvent” particles between two proteins causes an attractive force, is primarily responsible for phase separation. For one‐component models of protein solutions, the theory yields simple algebraic expressions for the equation of state and for the chemical potential of the protein. This analytical theory describes the observed solubility behavior of proteins, including the effect of protein and polymer size, protein charge and concentration, and concentration of simple electrolytes.
| Year | Citations | |
|---|---|---|
Page 1
Page 1