Why is a protein more soluble when the pH is greater than or less than its pI?

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Expert Solution

It is positively charged at low pH and negatively charged at high pH. ... In general, the net charge on the protein, either positive or negative, can interact with water molecules, meaning that it is more likely for a protein molecule to dissociate itself from other protein molecules, thus, more soluble.

It is positively charged at low pH and negatively charged at high pH. The intermediate pH at which a protein molecule has a net charge of zero is called the isoelectric point of that protein. ... As a result, amino acid is the least soluble when the pH of the solution is at its isoelectric point.

queen_honey_blossom answered 1 year ago

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