The rotation of the F0 rotor is driven by the proton gradient. Examine the F0 rotor of E. coli. The protons enter through the entry half-channel and are passed on to a(n) .The rotation of the F0 rotor is driven by the proton gradient. Examine the F0 rotor of E. coli. The protons enter through the entry half-channel and are passed on to a(n) .Arg residue on one "c" subunit’s C-terminal helixprotonated Asp residue on one "c" subunit’s C-terminal helixArg residue on the "a" subunit’s helix closest to the c-ringunprotonated Asp residue on one "c" subunit’s C-terminal helix

The elongation cycle is the productive phase of protein biosynthesis. The genetic message in the mRNA is a functional transcription of a gene in the DNA and is translated one triplet codon at a time during this phase.

After peptidyl transfer, the nascent polypeptide chain binds to the incoming tRNA, with its anticodon still at the A site of the 30S subunit. It must be moved to the P site along with the mRNA by exactly one codon. This is done by EF-G in the elongation translocation step,where EF-G pushes the tRNA and codon attached to the mRNA from the A site to the P site of the 30S subunit.After this, the GTP of EF-G is it is hydrolyzed to GDP in the GTPase center of the ribosome and EF-G GDP is released. The high level of GTP in the cell and the relatively low affinity of GDP for EF-G is sufficient to ensure that EF-G is reactivated.The process by which the growing polypeptide on the ribosome is lengthened by one amino acid depending on the codon in the mRNA involves the activities of the three elongation factors EF-Tu, EF-Ts,and EF-G. EF-Tu in its active complex with GTP interacts with any aa-tRNA and prevents spontaneous hydrolysis of the ester bond between the carboxyl acid residue of the amino acid and the 30-ribose terminal hydroxyls of the tRNA.

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