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7.4 - Translation

7.4 - Translation

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Published by IB Screwed
IB Biology notes for translation of proteins
IB Biology notes for translation of proteins

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Categories:Types, School Work
Published by: IB Screwed on Jun 11, 2011
Copyright:Attribution Non-commercial


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7.4 - Translation
7.4.1 - Explain that each tRNA molecule is recognised by a tRNA-activating enzyme that binds a specific amino acid to the tRNA, using ATP for energy
Each amino acid has a specific
tRNA-activating enzyme
. Before they are used in translation, amino acids are attached to a matching tRNA molecule. On the 3
 end of the molecules, the base sequence
 appears, which binds to the amino acid with the aid of the activating enzyme. The tRNA molecules recognise the correct amino acid due the variation in their shape. They will match to a certain enzyme. The attachment of the amino acid requires ATP for the enzyme to induce the reaction. The anticodon is three bases long, and uses complementary base pairing to match to the code on the mRNA molecule. Note that the DNA code is degenerate, since a single amino acid may bind to multiple tRNA molecules.
7.4.2 - Outline the structure of ribosomes, including protein and RNA composition, large and small subunits, three tRNA binding sites and mRNA binding sites
Ribosomes are primarily made up of two parts - the small subunit and the large subunit. The small subunit has the binding site for the mRNA molecule, whilst the large subunit has three binding sites for tRNA molecules. These three binding sites are called the E, P and A sites. Ribosomes are
for the translation of mRNA into a polypeptide. One ribosome may catalyse the translation of many different mRNA molecules.
7.4.3 - State that translation consists of initiation, elongation, translocation and termination
During this stage, the mRNA molecule and the tRNA molecule both bind to the ribosome for translation to begin. The first tRNA molecule to bind to the small subunit carries the anticodon for the start codon. The small subunit then attaches to the mRNA molecule at the 5
 end. The small subunit then slides along towards the 3
 end until it reaches the start codon, and translation begins.
The tRNA molecules will attach to the complementary bases on the mRNA, using codon to anticodon recognition. As this happens, the amino acids are brought together so that they can bond and form polypeptides. Once the amino acids form peptide bonds, they are detached from the tRNA by the large subunit. Throughout translation, the polypeptide will be held in position by a single tRNA molecule.
Within the ribosome, there are three areas called the E, P and A sites. During translation, the tRNA will move through this, depending on which stage of translation it is at. The tRNA first enters at the A site. Then, as the peptide bonds form, the molecule will move to the P site. Finally, it will move to the E site to be release.
Eventually, the ribosome will reach the
stop codon
 on the 3
 end of the mRNA. Since there are no tRNA molecules with an anticodon for it, translation will stop. The mRNA and the newly synthesised polypeptide are released from the ribosome. The tRNA is also released, which will be reused and attach to another amino acid. By this point, the polypeptide will have started to fold into the shape of the final protein. The subunits of the ribosome will also separate.

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