How do amino acids change at different pH?

Amino acids are amphoteric which means they can act as an acid or a base.

An isoelectric point is the pH at which an amino acid exists as its zwitterion. A zwitterion is the dipolar ionic form of an amino acid. This is formed by a hydrogen ion (H+) from the carboxyl group being donated to the amino group. There is no overall charge. The carboxyl group becomes COO- and the amino group becomes NH3+ showing an imbalance of charge that makes it a polar molecule.

If the pH is lower (in acidic conditions) than the isoelectric point then the amino acid acts as a base and accepts a proton at the amino group. This gives it a positive change.

If the pH is higher (in alkaline conditions) than the isoelectric point then the amino acid acts as an acid and donates a proton from its carboxyl group. This gives it a negative charge.

ZC
Answered by Zoe C. Chemistry tutor

73930 Views

See similar Chemistry A Level tutors

Related Chemistry A Level answers

All answers ▸

Describe the mechanism for bromination across a double bond


How do you work out the oxidation number of a atom in a compound?


Explain, in terms of frequencies, why solutions of transition metal ions are often coloured.


Explain why Carbon Dioxide has a linear shape with a bond angle of 180 degrees


We're here to help

contact us iconContact ustelephone icon+44 (0) 203 773 6020
Facebook logoInstagram logoLinkedIn logo

MyTutor is part of the IXL family of brands:

© 2025 by IXL Learning