After the start codon is seen on the mRNA, met-tRNA binds to the P site. Next, a peptide chain-tRNA binds to the A site, and the neighboring amino acids connect, forming a peptide chain.
A new amino acid-tRNA molecule enters the A site and binds with its anti-codon region matching the mRNA.
GTP and elongation factors help hold the tRNA at the A-site until the amino acids are linked.
While the new amino acid-tRNA molecule is at the A-site, the existing peptide chain binds the amino acid.
The peptide chain-tRNA molecule now moves to the P-site, after which tRNA breaks off from the peptide chain.
The free tRNA in the P-site moves to the E-site, where it is kicked off when a new tRNA brings in the next amino acid.
When the stop codon is encountered, termination is prompted. This codon is recognized by release factors, which then work to disassemble the ribosomal complex, which is bound to mRNA.
Stop codons are not recognized by tRNA, but rather by release factors. When the stop codon is encountered, these release factors work to disassociate the ribosomal complex from the mRNA it is bound to.
Shortly after disassociating from the mRNA, the ribosomal complex falls apart.
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