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Proteins
Proteins
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.
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.
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)