The addition of a small amount of a salt, such as (NH4)2SO4, to a solution containing a charged protein increases the solubility of the protein in water. This observation is called the salting-in effect. However, the addition of large amounts of salt can decrease the solubility of the protein to such an extent that the protein precipitates from solution. This observation is called the salting-out effect and is used widely by biochemists to isolate and purify proteins. Consider the equilibrium PXν(s) ⇋ Pν+(aq) + ν X−(aq), where Pν+ is a polycationic protein of charge ν+ and X− is its counterion. Use Le Chatelier’s principle and the physical principles behind the Debye–Hückel theory to provide a molecular interpretation for the salting-in and salting-out effects.
The addition of a small amount of a salt, such as (NH4)2SO4, to a solution containing a charged protein increases the solubility of the protein in water. This observation is called the salting-in effect. However, the addition of large amounts of salt can decrease the solubility of the protein to such an extent that the protein precipitates from solution. This observation is called the salting-out effect and is used widely by biochemists to isolate and purify proteins. Consider the equilibrium PXν(s) ⇋ Pν+(aq) + ν X−(aq), where Pν+ is a polycationic protein of charge ν+ and X− is its counterion. Use Le Chatelier’s principle and the physical principles behind the Debye–Hückel theory to provide a molecular interpretation for the salting-in and salting-out effects.
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