Lesson 1

Proteins
 Retrievalquestion
Retrieval answer 11 Retrieval
Retrievalquestion
answer 22

Draw and label a triglyceride Describe

Glycerol the structure
bonded by ester of a
bonds
to 2 fatty phospholipid
acids and a phosphate
group

Retrieval
Retrievalquestion
answer 33 Retrieval
Retrievalquestion
answer 44
Amylose (unbranched) –
State
Alphathe
glucose
monosaccharides
+ alpha glucose
that Describe the structure
alpha glucose bondedofbystarch
1,4-
make maltose glycosidic bonds.
Helix shape which surrounds
Amylopectin (branched) –
alpha glucose bonded by 1,4 and
1,6-glycosidic bonds
 Date: 28-Dec-22

State
describe
explain
 How does this learning link to GCSE?
CB1 – Specialised cells – red blood cell & haemoglobin, Enzymes – digestive enzymes, structure
and enzyme activity

How does this learning link to other topics in A

Level?
Hydrolysis and condensation reactions

How does this learning link to this topic?

Respiration
Photosynthesis

GCSE
CB1 – Enzymes
CB2 – Plant growth
CB3 DNA and genetics
CB6 – Mineral ions
What is the role of enzymes in
biological processes in the body and
how does their structure aide their
function?
Core Practical 1: Investigate a factor
affecting the initial rate of an enzyme
– controlled reaction
The Learning Journey of Topic 1 Biological Molecules
How does the structure of lipids help
Why is the folding of a protein
an organism with energy storage,
important for it’s function?
How is the structure of glucose, insulation and water proofing?
starch, glycogen and cellulose related
to their function ?
What types of mutations occur in
DNA and what diseases might they
cause?
How does the structure of DNA help
How are proteins manufactured in
to explain semi-conservative
the cell and what is RNA?
replication?
POST 18
What do plants need to grow?
Molecular biologist
Geneticist
Biochemist
Can you explain why the nature of Enzyme engineering scientist
water is important for all living Fermentation scientist
organisms? Enzymologist
Forensic scientist
Clinical laboratory technician
Research scientist
Take out your homework
Ester Bond
 1. Name the subunits of a
protein.
2. Name the enzyme that digests
a protein.
GCSE prior
3. Describe the test for the
knowledge – presence of protein.
White board
4. State the organelle where
time protein synthesis occurs.
5. State what determines the
sequences of amino acids
Proteins – (another organic molecule)

• Proteins make up about 2/3 of the total dry mass of

a cell.

• They differ from carbohydrates and lipids because

the contain NITROGEN and Sulphur.

• They also still contain Carbon, Hydrogen and

Oxygen.
Structure of Proteins

• Monomer units of proteins are called amino acids.

• There are 20 different amino acids

• Polymers are the peptides and proteins

• Amino acids combine to form long chains
therefore the variety of polypeptides is vast.

• Polypeptide and protein is used interchangeably

 Structure of Amino Acids
General formula = NH2 – CHR - COOH

H
H H
O
N C C
H O
AMINO GROUP
CARBOXYL
R-GROUP GROUP
(Variant)
 STRUCTURE OF AMINO ACIDS
General formula = NH2 – CHR - COOH

amino carboxylic
group acid group

R group
The R group represents a side chain from the central
‘alpha’ carbon atom, and can be anything from a simple
hydrogen atom to a more complex ring structure.
 Examples of different amino acids and their R groups
(No you do not need to learn these by heart)

• The R group determines the amino acid as it is different

for every amino acid.

Alanine
Glycine
Leucine
Linking different amino acids together in different
sequences produces proteins with different
properties.

This explains how the many proteins in an organism

can have so many different functions
Protein structure

• Two amino acids combine in a condensation

reaction to form a…
DIPEPTIDE

• The covalent peptide bond forms between the

AMINO group of one amino acid and the CARBOXYL
group of the other
Protein structure

• If another condensation reaction occurs then a…

TRIPEPTIDE is formed

• This is how you get long chains of amino acid

residues all linked by peptide bonds
 Have a go at combining two amino acids in a
condensation reaction

The covalent peptide bond forms between the AMINO

group of one amino acid and the CARBOXYL group of the
other
 Describe a peptide bond
The bond between two amino acids joining the amino group
from one amino acid to the carboxyl group of a second amino
acid formed through a condensation reaction
 AN AMINO ACID CAN IONISE.

amino carboxylic
group acid group

R group
Amino acids are amphoteric – They can ionise as both acid or
base.
An ion which contains both positive (carboxylic group) and
negative (amino group) charges is called a zwitterion (at pH 7)
Based on the
R Group
amino acids
can be polar
or nonpolar
Questions – Page 46 Q6
Lesson 2
 Structure of
proteins
The shape of the protein
is critical in determining
its properties

• Primary structure
• Secondary structure
• Tertiary structure
• Quaternary structure
 Structure of Proteins
PRIMARY STRUCTURE –
Polypeptides
• Polypeptides are
composed of amino acids
bonded to each other,
like beads on a string
• The bond that holds them
together is called a
peptide bond
• They are formed by loss
of water so is called a
condensation reaction.
 Primary structure

• The sequence of amino acids of the protein

• The order of amino acids is determined by the DNA of the
cell that is producing it (more of that later in the term!)
On your white boards, describe what is happening during
secondary structure
Secondary structure– Alpha Helix

• Carboxyl group (-ve) of 1 amino acid forms a

hydrogen bond with the Hydrogen of an amino
group (+ve) 4 amino acids down the chain.
Eg amino acid 1 bond to amino acid 5
• This bonding pulls the amino acids into a helix
shape.
Secondary structure– Beta-pleated sheet

• 2 or more alpha-
helix chains, line up
next to each other.
• Hydrogen bonds
form between
carboxyl and amino
groups. This forms a
backbone of the
beta –pleated sheet.
 • Secondary folding occurs immediately
after formation and refers to the folding
that occurs between atoms within the
polypeptide.
• It does not involve any bonding to the
R-groups.
• The most common secondary structures
Secondary are:
structure • Coiling → alpha helix
• Folding → beta pleated sheets
• These shapes are permanent
• They are held in place by hydrogen
bonds which form between the carbonyl
(C=O) O of one amino acid and the
amino (N-H) H on the other.
Modelling protein structure worksheet
 • Further folding to form the 3D
shape – (this is tertiary
structure).
• Compact structure of the protein
Tertiary • Unique to that protein. It is due
structure to interactions between the R
groups of the amino acids.
• Ionic bonds, hydrogen bonds
and disulphide bonds.
 • Disulphide bonds
• Strong, covalent and not easily
broken down.
• Oxidation of sulphur-containing side
chains of two cysteines.
• Ionic bonds
• Electrostatic interaction (+/-)
Tertiary between oppositely charged ions
• easily broken down by changes in
structure pH (carboxyl/amino groups)
• Hydrogen bonds
• Hydrogen atom is shared between
two atoms
• Weak
• But a lot of them together makes
them stronger
The 3D shape of a protein is maintained by several
types of bond, including:
Hydrophobic
Hydrogen bonds: interactions:
involved in all levels of between non-polar
structure. sections of the protein.

Disulfide bonds: one of the

strongest and most
important type of bond in
proteins. Occur between
two cysteine amino acids.
 • Some proteins are made up of
multiple polypeptide chains, also
known as subunits.
Quaternary
• When these subunits come
structure together, they give the protein
its quaternary structure.
• Forming a complex, biologically
active molecule