Amino acids are molecules that contain both acidic (carboxyl) and basic (amine) functional groups.

At a
neutral pH of 7.0, the carboxyl group is deprotonated (negatively charged) and the amino group is
protonated (positively charged). This results in an overall charge of zero and the amino acid is
considered a zwitterion.

The effect of pH on the zwitterion of an amino acid is related to the ionization of the carboxyl and amino
groups. As the pH of the solution changes, the relative concentrations of hydrogen ions (H+) and
hydroxide ions (OH-) also change. This affects the ionization state of the functional groups in the amino
acid.

At a low pH (acidic conditions), the concentration of H+ ions is high, causing the carboxyl group to be
protonated (positively charged) and the amino group to remain protonated (positively charged). As a
result, the overall charge of the amino acid becomes positive, and it is known as a cationic form.

At a high pH (alkaline conditions), the concentration of OH- ions is high, causing the carboxyl group to be
deprotonated (negatively charged) and the amino group to remain protonated (positively charged). As a
result, the overall charge of the amino acid becomes negative, and it is known as an anionic form.

At the isoelectric point (pI) of the amino acid, the net charge of the molecule is zero. This occurs when
the pH is equal to the average of the pKa values of the carboxyl and amino groups. At this point, the
amino acid exists as a zwitterion with equal numbers of positively and negatively charged groups.

In summary, the pH of the solution can have a significant effect on the charge of the zwitterion form of
an amino acid. At low pH, the amino acid exists in a cationic form, and at high pH, it exists in an anionic
form. At the isoelectric point, the amino acid exists as a zwitterion with no net charge.