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C/W Protein Structure

L.O.
We are learning about the different levels of protein
structure

Starter:
1. Complete the card sort activity on carbohydrates from
the previous lesson

2. Complete the multiple choice POP QUIZ!

Key words carbohydrate,


protein, aminomonosaccharide,
acid, amino group, carboxyl
carbon, group, R
polymer,
group, peptide
monomer, bond, primary,
polysaccharide, secondary,reducing
disaccharide, tertiary,sugar,
quarternary,
Benedicts
disulfide,-glucose,
solution, ionic, hydrogen.
-glucose, glycosidic bond.
Learning Outcomes
To be able to explain what is meant by a reducing
sugar

To be able to define primary, secondary, tertiary and


quaternary protein structure

To be able to describe and explain the four types of


bonds that helps give proteins their shape
To know how polypeptides are made.
To understand how polypeptides are arranged.
To understand how to test for proteins.

The structure of protein


An acidic group COOH.
amino acid
A basic group NH2.
polypeptide
A polymer made from amino acids.
amino group
A hydrogen atom H.
carboxyl group
Each amino acid has a different R
group made from different chemicals.
hydrogen atom
The monomer unit that makes up
R group
polypeptides.
To know how polypeptides are made.
To understand how polypeptides are arranged.
To understand how to test for proteins.

Key words protein, amino acid, amino group, carboxyl group, R group, peptide
bond, primary, secondary, tertiary, quarternary, disulfide, ionic, hydrogen.
Peptides

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Peptide bonds and dipeptides

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The 20 naturally-occurring amino acids

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All of the possible amino acid
R groups begin with a carbon-
carbon bond apart from
glycine, which has a hydrogen.

Key words protein, amino acid, amino group, carboxyl group, R group,
peptide bond, primary, secondary, tertiary, quarternary, disulfide, ionic,
The structure of proteins

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Polypeptides
When more amino acids
are added to a dipeptide,
a polypeptide chain is
formed.

A protein consists of one


or more polypeptide
chains folded into a highly
specific 3D shape.

There are up to four levels of structure in a protein: primary,


secondary, tertiary and quaternary. Each of these play an
important role in the overall structure and function of the
protein.

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Primary structure: - the sequence of amino acids in a
polypeptide chain

Secondary structure: - the formation of repeating patterns due to


hydrogen bonds between non-adjacent
amino acids, primarily -helixes and -
pleated sheets
-pleated sheet
- secondary structures form as a result of
-helixes
hydrogen bonding between different
amino acids in the chain
- hydrogen bonds can form:
the CO (carboxyl group) of one amino
-helix
acid and the NH (amine group) of
another amino acid
the CO of one amino acid and the OH
(hydroxyl group) of another amino acid
Portion of polypeptide chain

Amino Peptide
acids bond

Hydrogen
bonds form Hydroge
n bonds

- helix
Portion of polypeptide chain

Hydrogen
bonds form

Hydroge
n bonds

- pleated sheet
- pleated
sheet

Amorphou
- helices s regions

Tertiary structure
- The way in which a protein coils up
to form a precise three-dimensional
shape is its tertiary structure.
Forces responsible for the formation of tertiary structure:

Hydrogen bonds
Ionic bonds
Disulphide bonds
Hydrophobic interactions
between non-polar side
chains
Hydrogen bonds
Shared electrons spend longer at
bonds to these atoms, forming a slight
molecule negative charge

C
O- +H N bonds to
molecule
hydrogen
bond

High temperatures and altered pH can


split these bonds
These interactions are weak compared
to disulfide bonds
Ionic bonds

bond to
molecule O Basic group
C H
Acidic group O- +H N
bond to
H molecule
Ionic
bond

Ionic bonds can be split be changing


the pH
These interactions are weak compared
to disulfide bonds
Disulphide bonds
cysteine
R group

CH2 SH HS CH2

CH2 S S CH2
disulphide
bond

Disulfide bonds can be split be


reducing agents.

Disulfide bonds are the strongest of


the four interactions
Hydrophobic interactions
These are weak forces of attraction between non-polar
groups on the side chains
Water excluded from these hydrophobic side chains
helps keep the side chains together

Valine Phenylalanine
R group R group

CH(CH3)2 CH2

Weak van der Waals


force of attraction
These forces can be split by a rise in
temperature. They are the weakest of the four
interactions
Lysine Tyrosine Asparagine Serine
1 2 3 4 5 6 7 8 9 10 11 12 13 14

(CH2)4 CH2 Polar R CH2 CH2 Polar R 15


Basic R
group C OH group
group +NH
3 O NH2 16

Non-polar
OH R group CH3 17

Polar R
group Histidine 18
+HN NH
Polar R
38
Non-polar group CH2 19

R group
37 CH3 HS CH2 20

36 35 34 33 32 31 30 29 28 27 26 25 24 23 22 21

Alanine CH2 Acidic R CH2


Cysteine group C Aspartate
SH -O O
1 2 3 4 5 6 7 8
9
(CH2)4 CH2 CH2
C 10
Ionic +NH
3 O NH2
bond O- O
C HO HO CH2 11
HN
CH2 12

24 HN Hydrogen
13
23 CH2 bonds
25 22
21 20 19 18 17 16 15 14

26 Disulphid CH2 CH3


27 e bond
S CH3 van der Waals
28
S 34 forces
29 CH2 33 35

30 31 32 36 37 38
Quaternary structure
- Some proteins consist of more than one polypeptide
chain held together in a precise three-dimensional
structure
- Two or more polypeptide chains are held together
gives a proteins quaternary structure. They are held
together by the same type of forces responsible for
the formation of tertiary structures
- Quaternary structures can also involve the additional of
non-amino acid derived groups known as prosthetic
groups
These prosthetic groups can be formed
from metal ions, sugars, vitamins, methyl
groups, phosphate groups, etc..
Bonds in proteins
The 3D shape of a protein is maintained by several types of
bond, including:
hydrogen bonds: hydrophobic
involved in all levels of interactions:
structure. between non-polar
sections of the protein.

disulfide bonds: one of


the strongest and most
important type of bond in
proteins. Occur between
two cysteine amino acids.

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Protein structure

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TASK:
Your task is to create two flash cards. One on the four
types of protein structure and one of the four types of
bonds that give proteins their 3D shape. To include:
Protein structures:
- Definition of primary, secondary, tertiary and quaternary
structures.
- The names of the two types of secondary structures.
- The names of the bonds involved in each level
Bonds:
-the four different types of bond
-how and where they form (between which groups on the
side chains)
-a simple diagram
-are they weak or strong
To be able to explain what is meant by a reducing sugar
To be able to define primary, secondary, tertiary and quaternary protein structure
To be able to describe and explain the four types of bonds that helps give proteins their
shape

What have we learned so far?

Quick quiz!

Key words protein, amino acid, amino group, carboxyl group, R group, peptide
bond, primary, secondary, tertiary, quarternary, disulfide, ionic, hydrogen.
Biuret test for proteins

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Mystery substance

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Multiple-choice quiz

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To be able to explain what is meant by a reducing sugar
To be able to define primary, secondary, tertiary and quaternary protein structure
To be able to describe and explain the four types of bonds that helps give proteins their
shape

I dont know anything


I will school you
about proteins
on proteins sir

Now work on the past paper questions at


the back of your work booklets

Key words protein, amino acid, amino group, carboxyl group, R group, peptide
bond, primary, secondary, tertiary, quarternary, disulfide, ionic, hydrogen.
To know how polypeptides are made.
To understand how polypeptides are arranged.
To understand how to test for proteins.

Random plenary
generator.

Key words protein, amino acid, amino group, carboxyl group, R group,
peptide bond, primary, secondary, tertiary, quarternary, disulfide, ionic,