Question

Enantiomers, like L-alanine and D-alanine, are so similar that ribosomes will incorporate either one into a protein during synthesis. True or False?

Answer 1

False

Answer 2

true

Answer 3

[AI-generated answer — Explain Bot]

False.

Enantiomers, such as L-alanine and D-alanine, are mirror images of each other and have identical physical and chemical properties, except for their interaction with polarized light. However, their different three-dimensional structures can have significant biological implications.

The specificity of protein synthesis is governed by the interactions between the tRNA molecules and the codons on mRNA during ribosomal translation. The tRNA molecules have specific anticodons that match the codons on mRNA, ensuring the correct amino acid is incorporated into the growing protein chain. In this process, the ribosome selects the appropriate amino acid-tRNA complex based on complementarity between the codon and anticodon sequences.

Since L-alanine and D-alanine have mirror-image structures, they have different chirality, meaning their anticodons in tRNA will not be complementary to the codons on mRNA. As a result, ribosomes will only incorporate the specific enantiomer that is encoded by the genetic code in protein synthesis.

Therefore, ribosomes cannot incorporate both L-alanine and D-alanine indiscriminately into a protein during synthesis. The specificity arises from the molecular recognition between a specific codon and its corresponding anticodon, ensuring the accurate incorporation of the correct enantiomer during protein synthesis.