1. A molecule of mRNA has been produced via transcription and has left the nucleus via a
nuclear pore. This mRNA carries a sequence of codons which codes for the amino acid
sequence of the specific protein which will now be synthesised by translation. (Each mRNA
codon of three bases codes for one specific amino acid.) This mRNA moves into the cytoplasm;
a ribosome attaches to the mRNA, at the start codon (which is always AUG).
2. There are two binding sites for tRNA molecules within the ribosome, because two mRNA
codons (i.e. six bases) are held within the ribosome at one time.
3. The first tRNA arrives; it is carrying a specific amino acid and has an anticodon of three
bases which are complementary to the first codon of the mRNA. The anticodon of the tRNA
binds to the complementary mRNA codon, via hydrogen bonding between complementary
bases pairs.
4. The second tRNA arrives, occupying the second binding site within the ribosome; it is
carrying a specific amino acid. The anticodon of this tRNA binds to the second codon of the
mRNA, via hydrogen bonding between complementary pairs of bases.
5. Now that two tRNA molecules are sitting side by side within the ribosome, the amino acids
they are carrying are brought into close proximity. An enzyme called peptidyl transferase
catalyses the formation of a peptide bond between the two amino acids, via a condensation
reaction (which also releases a molecule of water). The peptidyl transferase enzyme is part of
the ribosome.
6. As the peptide bond is forming, the first amino acid is released from the first tRNA. The
second tRNA is still carrying its amino acid, but this is now joined to the first amino acid as a
dipeptide.
7. The ribosome moves along the mRNA by a distance of one codon. This causes the first tRNA
to be released back into the cytoplasm. (It will be reused, i.e. another amino acid of the same
specific type will be attached to it.)
8. The third codon of the mRNA has now been brought into the ribosome. A tRNA, carrying a
specific amino acid, will arrive and its anticodon will bind to the mRNA codon, via hydrogen
bonds between complementary bases.
9. A peptide bond forms between the amino acid carried by this (third) tRNA and the amino
acid which is still attached to the second tRNA, forming a tripeptide. The reaction is catalysed
by peptidyl transferase.
10. The ribosome moves along the mRNA by a distance of one codon, causing the release of
the second tRNA (which has released its amino acid); the fourth mRNA codon is now brought
within the ribosome.
11. The process repeats, with further amino acids being added to the chain, forming a
polypeptide. Each mRNA codon codes for one specific type of amino acid, hence the order of
mRNA codons has determined the order in which amino acids have been joined in the
polypeptide chain, i.e. the primary structure of the protein).
12. Eventually, the ribosome reaches a stop codon in the mRNA. This codon does not code for
any amino acid, hence it marks the end of the translation of the encoded polypeptide. The
ribosome now detaches from the mRNA and the polypeptide chain, now complete, is also
released.
13. The secondary structures of the protein begin to fold even before the complete polypeptide
has been synthesised: some parts of the chain coil into α‐helix, whilst other parts fold back on
themselves to form β‐pleated sheet. These secondary structures are held in place by hydrogen
bonding between δ+ hydrogen atoms (from N‐H groups) and δ‐ oxygen atoms (from C=O
groups) that are found in different parts of the backbone of the same polypeptide chain.
14. Tertiary structure may also start to form before the synthesis of the polypeptide chain is
complete. Tertiary structure is the further folding of the polypeptide chain (which has already
formed regions secondary structure) into its final 3D shape. The types of amino acid R groups
present determine which types of bonding form; this in turn determines the tertiary structure
(3D shape) that forms. The relevant types of bond between R groups include disulphide
bridges, hydrogen bonding, ionic bonding and hydrophobic interactions.
15. Many proteins are not complete and functional until they have gone further (posttranslational)
modifications or processing. These modifications typically occur in the Golgi
apparatus; newly synthesised proteins are transported to the Golgi in vesicles. The types of
modification that can occur include: attachment of a prosthetic group (e.g. a haem group),
association of more than one polypeptide chain to form a protein with quaternary structure
and attachment of carbohydrate to a protein to form glycoprotein. Specific amino acids may
also be removed from a protein to produce its final, functional form.