Final answer:
Orthogonality in biochemical interactions, such as those between aaRS and tRNA, ensures specificity in aminoacylation and is necessary for correct protein synthesis. These interactions are true manifestations of biochemical orthogonality.
Step-by-step explanation:
Orthogonality in the context of biochemistry refers to the specificity and independence of interactions, such as those between aminoacyl-tRNA synthetases (aaRS) and tRNA molecules in protein synthesis. Biochemical interactions between aaRS enzymes and their corresponding tRNA molecules are crucial for the correct aminoacylation of tRNAs, thus ensuring that the correct amino acid is added to the growing polypeptide chain during translation. Stereochemical interactions play a significant role in this specificity, and aaRS enzymes exhibit high selectivity for their cognate tRNA and amino acid substrates. The coevolution of aaRS and tRNA is suggested by structural homologies and editing functions that further enhance the accuracy of protein synthesis.
Therefore, the statement that orthogonality is made possible by the biochemistry of aaRS-tRNA interactions is True, as these complex interactions ensure the fidelity of the genetic code through highly specific mechanisms.