A dipeptide is formed through a condensation reaction between the amino group of one amino acid and the carboxyl group of a second amino acid, releasing water and creating a peptide bond. The correct dipeptide structure maintains a free amino group on the N-terminal end and a free carboxyl group on the C-terminal end.
Two amino acids combine to form a dipeptide when the amino group of one reacts with the acid group of the other, releasing a molecule of water in a process known as a condensation reaction. The correct structure for a dipeptide is one where the nitrogen atom (N) of the amino group from the first amino acid forms a peptide bond with the carbon atom (C) of the carboxyl group from the second amino acid. This bond is called a peptide bond, which is a type of amide bond. The two linked amino acids will still have terminal groups available for further reaction: a free amino group on one end (N-terminal) and a free carboxyl group on the other end (C-terminal).
The formation of a dipeptide is a key step in producing polypeptides and eventually proteins. Repeating this condensation reaction will lengthen the peptide chain, potentially creating polypeptides that are large enough to become functional proteins. The sequence in which the amino acids are joined, with the free amino group on the left (N-terminal) and the free carboxyl group on the right (C-terminal), is a convention in the representation of peptide structure.
The complete question is -Two amino acids combine to form a dipeptide when the amino group of one reacts with the acid group of the other. Which structure is correct? options in image.