Final answer:
Amino acids are more soluble in aqueous solvent at pH extremes due to their charged nature, which increases their solubility in polar solvents. The neutral charge of an amino acid at its isoelectric point makes it hydrophobic and less soluble. At very low or very high pH, amino acids have increased charge and form more salt bonds with water, increasing their solubility.
Step-by-step explanation:
This phenomenon can be explained by the properties of amino acids at different pH values. At the isoelectric point (pI), the amino acid is neutral, which makes it hydrophobic and less soluble in water (option A). At pH extremes, the amino acid molecules mostly carry a net charge, which increases their solubility in polar solvents (option B). In addition, at very low or very high pH, the amino acid molecules have increased charge and form more salt bonds with water solvent molecules, further enhancing their solubility (option C).