Peptide bonds are formed between:

Explanation

The correct option is: Carboxyl groups and amino groups.Peptide bonds are formed through a condensation reaction between the carboxyl group (-COOH) of one amino acid and the amino group (-NH2) of another amino acid. During this reaction, a water molecule is eliminated, and the carboxyl group and the amino group join together to form a peptide bond (-CO-NH-).Here's an explanation of the other options:Hydrogen groups of adjacent amino acids: Hydrogen atoms do not participate directly in the formation of peptide bonds. While hydrogen atoms are present in amino acids, they do not form covalent bonds during peptide bond formation.Non-functional groups of the amino acids: The term "non-functional groups" is a bit vague. Amino acids consist of various functional groups, such as carboxyl, amino, side chain (R-group), and others. However, only the carboxyl and amino groups specifically participate in peptide bond formation.Functional groups and hydrogen groups of adjacent amino acids: Peptide bonds are not formed between functional groups and hydrogen groups of adjacent amino acids. As mentioned earlier, the carboxyl and amino groups directly participate in peptide bond formation, while hydrogen groups (hydrogen atoms) do not form covalent bonds during this process.To summarize, peptide bonds are specifically formed between the carboxyl group of one amino acid and the amino group of another amino acid, resulting in the formation of a peptide chain.