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Hi guys, could you help answer this!

n E. coli, the elongation factor EF-Tu forms part of an EF-TuGTPtRNA complex and increases the rate of tRNAmRNA binding. GTP hydrolysis to GDP and Pi also enables a type of kinetic proofreading, which prevents the addition of an incorrect amino acid to the growing peptide chain. Determine which of the following statements are true. Check all the true statements.

In E. coli, the elongation factor EF-Tu forms part of an EF-Tu?-GTP?-tRNA complex and increases the rate of tRNA-mRNA binding. GTP hydrolysis to GDP and Pi also enables a type of kinetic proofreading, which prevents the addition of an incorrect amino acid to the growing peptide chain. Determine which of the following statements are true. Check all the true statements. GDP-Ef-Tu must leave the ribosome before aminoacyl-tRNA can bind to the P site. A mismatch between the codon and anticodon does not cause conformational changes, and the Ef-Tu-GTP-aminoacyl-tRNA complex leaves the ribosome before a peptide bond can form. A correct match between the codon and anticodon causes a conformational change in the small ribosomal subunit and leads to GTP hydrolysis. A mismatch between the codon and anticodon creates a distortion in the mRNA-tRNA complex. An EF-Tu conformation change results in Ef-Tu-GDP exiting the ribosome and leaving behind the aminoacyl-tRNA. Hydrolysis of GTP associated with EF-Tu brings about a conformational change in the amino acid.

 

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