Within an alpha helix segment of a protein, which interaction primarily holds the coiled shape in place?

Core Concept

Secondary structure is a regular folding pattern stabilized by the chain's own repeated framework. In an alpha helix, the C=O group of one peptide bond accepts a hydrogen bond from the N-H group of another peptide bond located about four residues along the chain. These uniform contacts zip the backbone into a right-handed coil while side chains project outward, free to contact other parts of the protein or environment. Disrupting this backbone pairing unwinds the helix without breaking any covalent bond.