Which structural feature connects amino acids in a protein?

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The linking of amino acids in a protein is accomplished by a peptide bond, a covalent amide linkage formed when the carboxyl group of one amino acid reacts with the amino group of the next, releasing water. This creates the protein’s backbone and a repeating sequence of N-C-C units. The bond has partial double-bond character from resonance, making it planar and restricting rotation, which helps the chain adopt specific shapes necessary for folding into secondary and tertiary structures. Hydrogen bonds stabilize those folded structures but do not covalently connect amino acids in the chain. Glycosidic bonds join sugar molecules, and ester bonds link acids to alcohols, not the amino acids in a peptide chain.