Protein
Spec reference: 3.1.4.1
Amino acids are the monomers from which proteins are made. The general structure of an
amino acid as:
Where NH2 represents an amine group, COOH represents a carboxyl group and R represents a
side chain. The twenty amino acids that are common in all organisms differ only in their side
group.
A condensation reaction between two amino acids forms a peptide bond.
● Dipeptides are formed by the condensation of two amino acids.
● Polypeptides are formed by the condensation of many amino acids.
A functional protein may contain one or more polypeptides.
The role of hydrogen bonds, ionic bonds and disulphide bridges in the structure of proteins.
SPEC REFERENCE
Disulphide bridges: Fairly strong and therefore not easily broken. Bonds can be split by reducing
agents.
Ionic bonds: Formed between any carboxyl and amino groups that are not involved in forming
peptide bonds. They're weaker than disulphide bridges and are easily broken by changes in pH.
Hydrogen bonds: which are numerous but easily broke.
Proteins have a variety of functions within all living organisms. The relationship between
primary, secondary, tertiary and quaternary structure, and protein function.
The primary structure of a protein is the sequence of amino acids that make up its polypeptide
chains
The secondary structure: Polypeptides become twisted or coiled. These shapes are known as
the secondary structure. There are two common secondary structures; the α-helix and the
β-pleated sheet.
Tertiary structure - Secondary structures twist/fold even more to give 3D shape.
Shape held in place by:
- Disulphide bridges.
- Ionic bonds.
- Hydrogen bonds.
- Hydrophobic/hydrophillic interactions.
(Textbook) → the α-helix of the secondary structure can be twisted and folded even more to
give the complex, often specific, 3-D structure of each protein.
Polypeptide chains are held together in these quaternary structures by the same type of forces
responsible for the formation of tertiary structures.
→ Quaternary structures can also involve the addition of non-amino derived group known as
prosthetic groups.
The biuret test for proteins.
1 - Place a sample of the solution in a test tube and add an equal volume of sodium hydroxide
solution at room temperature.
2 - Add a few drops of dilute (0.05%) copper (II) sulphate solution and mix gently.
3 - A purple colouration indicates the presence of peptide bonds and hence a protein. If no
protein is present, the solution remains blue.
Globular proteins:
● Have complex tertiary and sometimes
the quaternary structures.
● Folded into spherical (globular) shapes.
● Usually double as hydrophobic side
chains in centre of structure.
● Roles in metabolic reactions.
Fibrous proteins:
● Little or no tertiary structure.
● Long parallel polypeptide chains.
● Cross linkage at intervals forming long
fibres or sheets.
● Hydrophilic amino acids are found on
the inside of the molecule and
hydrophobic on the outside,
● Usually insoluble.
● Many have structural roles.
● E.g. keratin in hair and the outer layer of
skin, collagen ( a connective tissue)
