Final answer:
GTP hydrolysis during translation is critical for the elongation stage, powering the binding and positioning of charged tRNAs within the ribosome and subsequently allowing for translocation and peptide bond formation.
Step-by-step explanation:
Hydrolysis of GTP attached to EF-Tu during translation facilitates the correct positioning and binding of a charged tRNA to the A site of the ribosome. This hydrolysis is necessary for the elongation phase of protein synthesis, ensuring the ribosome properly reads the mRNA codons and the polypeptide chain is extended accurately.
Each elongation cycle in protein synthesis consumes two GTP molecules: one for the delivery and binding of the aminoacyl-tRNA to the A site and another for translocation of the ribosome. After the formation of a peptide bond, which is catalyzed by peptidyl transferase, powered by the high-energy bond of the amino acid to its tRNA, the tRNA at the P site, now uncharged, moves to the E site and is ejected, making room for the next charged tRNA to enter at the A site.
Overall, the hydrolysis of GTP is a crucial energy source for the conformational changes and movements necessary during the translation process, enabling the ribosome to synthesize proteins efficiently.