Final answer:
During elongation in translation, peptidyl transferase catalyzes the formation of a peptide bond between the amino acids in the P and A sites at the ribosome. A peptidyl-tRNA with an ether bond in the P site would be less susceptible to nucleophilic attack compared to an ester bond.
option cis the correct
Step-by-step explanation:
In translation, during elongation process at the ribosome, a peptidyl-tRNA in the P site forms a peptide bond with the amino acid attached to the A-site tRNA. This reaction is catalyzed by the enzyme peptidyl transferase, which is integrated into the ribosomal subunit. Peptidyl transferase forms a bond between the carboxyl group of the amino acid in the P-site and the amino group of the amino acid in the A-site.
Now, coming to the strange modification with an ether versus an ester bond to the tRNA, the presence of an ether bond in the peptidyl-tRNA in the P site would make it less susceptible to nucleophilic attack.
This is because ether bonds are generally more stable and less reactive compared to ester bonds, which makes the peptidyl-tRNA molecule less susceptible to chemical reactions involving nucleophilic attack.