An amino acid is usually more soluble in aqueous solvent at pH extremes than it

Question

An amino acid is usually more soluble in aqueous solvent at pH extremes than it is at a pH near the isolelectric point of the amino acid. (Note that this does not mean that the amino acid is insoluble at a pH near its pI.)

Which of the following statements correctly explains this phenomenon?

(Select all that apply.)

The neutral charge of an amino acid molecule at its isoelectric point will make the molecule hydrophobic.

At pH extremes, the amino acid molecules mostly carry a net charge, thus increasing their solubility in polar solvent.

At very low or very high pH, the amino acid molecules have increased charge, thus form more salt bonds with water solvent molecules.

At pH values far from the isoelectric point, individual amino acid molecules have greater kinetic energy, thus more readily stay in solution.

Explanation / Answer

An amino acid is usually more soluble in aqueous solvent at pH extremes than it

Related Questions

Navigate

• Browse (All)
• Browse A
• Subjects

Integrity-first tutoring: explanations and feedback only — we do not complete graded work. Learn more.