Amino Acids & the Peptide Bond (Cambridge (CIE) AS Biology): Revision Note

Exam code: 9700

Cara Head

Written by: Cara Head

Reviewed by: Alistair Marjot

Updated on

Amino acids & the peptide bond

Proteins

  • Proteins are polymers (and macromolecules) made of monomers called amino acids

  • The sequence, type and number of the amino acids within a protein determines its shape and therefore its function

  • Proteins are extremely important in cells because they form all of the following:

    • Enzymes

    • Cell membrane proteins (e.g. carrier)

    • Hormones

    • Immunoproteins (e.g immunoglobulins)

    • Transport proteins (e.g haemoglobin)

    • Structural proteins (e.g keratin, collagen)

    • Contractile proteins (e.g. myosin)

Amino acids

  • Amino acids are the monomers of proteins

  • There are 20 amino acids found in proteins common to all living organisms

  • The general structure of all amino acids is a central carbon atom bonded to:

    • An amine group -NH2

    • A carboxylic acid group -COOH

    • A hydrogen atom

    • An R group (which is how each amino acid differs and why amino acid properties differ e.g. whether they are acidic or basic or whether they are polar or non-polar)

Diagram of an amino acid structure, showing an amino group, carboxyl group, and variable R-group side chain. Labels indicate basic and acidic groups.
The generalised structure of an amino acid

The peptide bond

  • In order to form a peptide bond a hydroxyl group (-OH) is lost from the carboxylic group of one amino acid and a hydrogen atom is lost from the amine group of another amino acid

  • The remaining carbon atom (with the double-bonded oxygen) from the first amino acid bonds to the nitrogen atom of the second amino acid

  • This is a condensation reaction so water is released

  • The resulting molecule is a dipeptide

  • When many amino acids are bonded together by peptide bonds the molecule formed is called a polypeptide

    • A protein may have only one polypeptide chain or it may have multiple chains interacting with each other

  • During hydrolysis reactions polypeptides are broken down to amino acids when the addition of water breaks the peptide bonds

Diagram showing amino acids forming a dipeptide via a peptide bond through condensation, with hydrolysis as the reverse process, involving water molecules.
Amino acids are bonded together by covalent peptide bonds to form a dipeptide in a condensation reaction

Examiner Tips and Tricks

You will be expected to recognise whether an unfamiliar molecule is an amino acid or protein so look for the functional groups (amine and carboxyl).

When asked to identify the location of the peptide bond, look for where nitrogen is bonded to a carbon which has a double bond with an oxygen atom, note the R group is not involved in the formation of a peptide bond.

You will also be expected to draw the general structure of an amino acid so be sure to practise this skill lots.

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Cara Head

Author: Cara Head

Expertise: Biology & Psychology Content Creator

Cara graduated from the University of Exeter in 2005 with a degree in Biological Sciences. She has fifteen years of experience teaching the Sciences at KS3 to KS5, and Psychology at A-Level. Cara has taught in a range of secondary schools across the South West of England before joining the team at SME. Cara is passionate about Biology and creating resources that bring the subject alive and deepen students' understanding

Alistair Marjot

Reviewer: Alistair Marjot

Expertise: Environmental Systems and Societies & Biology Content Creator

Alistair graduated from Oxford University with a degree in Biological Sciences. He has taught GCSE/IGCSE Biology, as well as Biology and Environmental Systems & Societies for the International Baccalaureate Diploma Programme. While teaching in Oxford, Alistair completed his MA Education as Head of Department for Environmental Systems & Societies. Alistair has continued to pursue his interests in ecology and environmental science, recently gaining an MSc in Wildlife Biology & Conservation with Edinburgh Napier University.