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This is because of the charge the salt can bring on the protein making it either likely or less likely interacted with water.
"The protein structure can also have an affect with it hydophobicity with hydrophobic patches on it (caused by the side chains Phe, Tyr, Leu, Ile, Met & Val). So the optimum salt is one that will cause hydration of the polar regions and dehydration of the hydrophobic regions of the protein. With which the salt does not interact directly with the protein. The best salts have a multivalent anions like sulphate or phosphate with cations like sodium or ammonium."(Scopes, 1994)
Ion Exchanges
The Ion exchanges exploit the different net charges on proteins at a given pH and interact with the proteins on electrostatic attraction (Scopes, 1994)...
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