At the isoelectric point, protein have no net charges and therefore will be less soluble. Why does increasing ionic strength result in an increase in solubility? Do the ions form a solvation shell?
Also when salting out the ionic strength of the solution is increase (salt = more ions) and this results in a precipitate. The ions disrupt the protein/solvent interaction and cause the protein to aggregate and therefore precipitate out.
Can someone please help explain this concept of protein solubility with ionic strength at isoelectric point. Thanks
