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

74802 Views

See similar Chemistry A Level tutors

Related Chemistry A Level answers

All answers ▸

Why do the atomic radii of the elements decrease across a period?


How do i know what the major and minor products of the reaction between Hydrogen Bromide and Propene would be?


What is Le Chatelier's principle?


What is solvent leveling? How can we distinguish between two strongly acidic solutions? (This is a challenging question and is included for interest only)


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