COMMONWEALTH OF AUSTRALIA

Copyright Regulations 1969

WARNING
This material has been reproduced and communicated to you by or on behalf of
La Trobe University pursuant to Part VB of the Copyright Act 1968 (the Act).
The material in this communication may be subject to copyright under the Act.
Any further reproduction or communication of this material by you may be the
subject of copyright protection under the Act.
Do not remove this notice.

Slide 1
 Amino acids –
general features
Module 3: Basics of protein building

Dr. Katrina Binger

Department of Biochemistry and Genetics Slide 2

Intended Learning Outcomes
(ILOs)
After this lesson students will be able to:
• Draw the general structure of an amino acid.
• Explain how a peptide bond is formed between two
amino acids, and how it can be broken.
• Describe the general structural features of a
polypeptide chain.

Slide 3
Amino acids: overview

• There are 20 amino acids

which are covalently joined
together during translation into
a polypeptide chain.
• The order, combination and
number of amino acids in a
polypeptide chain dictates a
proteins structure and function.
All 20 amino acids have the
same basic structure
α-carbon

Backbone

Note: only the R-group

differs between amino acids

Slide 5
Dehydration reaction between the carboxyl
and amino group of adjacent amino acid

• There are 20 amino

acids which are
covalently joined
together during
translation into a
polypeptide chain.
• Dehydration
reaction gives off a
water (H2O)
molecule.

Slide 6
Peptide bond joins amino acids together

Peptide bond

No matter what length the polypeptide chain, this pattern always repeats

Slide 7
Primary structure = sequence of
amino acids

• The start of every polypeptide chain

begins with a free NH2 group, so this
is called the Amino or N terminus
• The end of every polypeptide chain
ends with a free COOH group, so this
is called the Carboxyl or C terminus

Slide 8
Peptide bonds can only be broken by
hydrolysis: either by acids or proteases

Peptide bond

Acid hydrolysis Proteases

• Strong acid (e.g. HCl) + heat • Enzymes which cut peptide bonds
• All peptide bonds are cleaved • Specific to amino acid sequence,
non-specifically e.g. Trypsin cleaves after Arg or Lys

Slide 9
Summary

• All 20 amino acids share a common backbone, consisting of

amino and carboxyl termini, and a central alpha-carbon
• Amino acids are covalently joined together by a dehydration
(loss H2O) reaction between the carboxy terminus and
adjacent amino terminus
• Linked amino acids are a polypeptide chain; always
beginning with an N-terminus, and ending with a C-terminus

• Peptide bonds can only be broken by acid- or enzyme-

catalysed hydrolysis

Slide 10
Resources

• Lehninger Principles of Biochemistry Seventh

Edition (2017), W. H. Freeman and Company
• Chapter 3.1, 3.2

Slide 11