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Launchpad OCR A Level Biology Revision Notes

1. Development o… Protein: Structure

Author Last updated
Lára 31 May 2022
2. Foundations in …

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2.1 Cell Struc…

Levels of Protein Structure

2.2 Biologica…
There are four levels of structure in proteins, three are related to a
single polypeptide chain and the fourth level relates to a protein that
has two or more polypeptide chains
2.2.1 Properties of
Polypeptide or protein molecules can have anywhere from 3 amino
Water
acids (Glutathione) to more than 34,000 amino acids (Titan) bonded
together in chains

2.2.2 Monomers &

Primary structure
Polymers
The sequence of amino acids bonded by covalent peptide bonds is
the primary structure of a protein
The DNA of a cell determines the primary structure of a protein by
2.2.3 Monosaccharides
instructing the cell to add certain amino acids in specific quantities in
a certain sequence. This a!ects the shape and therefore the function
of the protein
2.2.4 The Glycosidic
The primary structure is specific for each protein (one alteration in the
Bond
sequence of amino acids can a!ect the function of the protein)

2.2.5 Polysaccharides

2.2.6 Biochemical

Tests: Reducing Sugars

& Starch

2.2.7 Lipids & Ester

Bonds

2.2.8 Lipids: Structure

& Function

2.2.9 Biochemical

Tests: Lipids

2.2.10 Amino Acids &

Peptide Bonds

The primary structure of a protein. The three-letter abbreviations

indicate the specific amino acid (there are 20 commonly found in cells
2.2.11 Protein: Structure
of living organisms).

2.2.12 Globular

Proteins Secondary structure

The secondary structure of a protein occurs when the weak
negatively charged nitrogen and oxygen atoms interact with the weak
2.2.13 Fibrous Proteins positively charged hydrogen atoms to form hydrogen bonds
There are two shapes that can form within proteins due to the
hydrogen bonds:
2.2.14 Inorganic Ions α-helix
β-pleated sheet

2.2.15 Biochemical The α-helix shape occurs when the hydrogen bonds form between
Tests: Proteins every fourth peptide bond (between the oxygen of the carboxyl
group and the hydrogen of the amine group)
The β-pleated sheet shape forms when the protein folds so that two
2.2.16 Finding the parts of the polypeptide chain are parallel to each other enabling
Concentration of a hydrogen bonds to form between parallel peptide bonds

Substance Most fibrous proteins have secondary structures (e.g. collagen and
keratin)
The secondary structure only relates to hydrogen bonds forming
2.2.17 Chromatography between the amino group and the carboxyl group (the ‘protein
backbone’)
The hydrogen bonds can be broken by high temperatures and pH
changes
2.3 Nucleoti…

2.4 Enzymes

2.5 Biologic…

2.6 Cell Divis…

3. Exchange & Tr…

4. Biodiversity, E…

5. Communicatio…

6. Genetics, Evol…
The secondary structure of a protein with the α-helix and β-pleated
sheet shapes highlighted. The magnified regions illustrate how the
hydrogen bonds form between the peptide bonds.

Tertiary structure
Further conformational change of the secondary structure leads to
additional bonds forming between the R groups (side chains)
The additional bonds are:
Hydrogen (these are between R groups)
Disulphide (only occurs between cysteine amino acids)
Ionic (occurs between charged R groups)
Weak hydrophobic interactions (between non-polar R groups)

This structure is common in globular proteins

The tertiary structure of a protein with hydrogen bonds, ionic bonds,

disulphide bonds and hydrophobic interactions formed between the R
groups of the amino acids.

Disulphide
Disulphide bonds are strong covalent bonds that form between two
cysteine R groups (as this is the only amino acid with a sulphur atom)
These bonds are the strongest within a protein but occur less
frequently, and help stabilise the proteins
These are also known as disulphide bridges
Disulphide bonds can be broken by oxidation
This type of bond is common in proteins secreted from cells eg. insulin

Ionic
Ionic bonds form between positively charged (amine group -NH3+)
and negatively charged (carboxylic acid -COO-) R groups
Ionic bonds are stronger than hydrogen bonds but they are not
common
These bonds are broken by pH changes

Hydrogen
Hydrogen bonds form between strongly polar R groups. These are
the weakest bonds that form but the most common as they form
between a wide variety of R groups

Hydrophobic interactions
Hydrophobic interactions form between the non-polar
(hydrophobic) R groups within the interior of proteins

Tertiary structure determines function

A polypeptide chain will fold di!erently due to the interactions (and
hence the bonds that form) between R groups
Each of the twenty amino acids that make up proteins has a unique R
group and therefore many di!erent interactions can occur creating a
vast range of protein configurations and therefore functions

The interactions that occur between the R groups of amino acids

determines the shape and function of a protein. These interactions are
found within tertiary structures of proteins.

Quaternary structure
Quarternary structure exists in proteins that have more than one
polypeptide chain working together as a functional macromolecule,
for example, haemoglobin
Each polypeptide chain in the quaternary structure is referred to as a
subunit of the protein

The quaternary structure of a protein. This is an example of haemoglobin

which contains four subunits (polypeptide chains) working together to
carry oxygen.

Summary of Bonds in Proteins Table

Examiner Tip
Familiarise yourself with the di!erence between the four structural levels
found in proteins, noting which bonds are found at which level. Remember
that the hydrogen bonds in tertiary structures are between the R groups
whereas in secondary structures the hydrogen bonds form between the
amino and carboxyl groups.

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2.2.10 Amino Acids & Peptide Bonds 2.2.12 Globular Proteins

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