An alpha helix is a coiled protein secondary structure with a repeated pattern of backbone hydrogen bonds. In the standard pattern, the backbone group of amino acid residue bonds to that of residue : for example, positions 2 and 6. This is an additional spatial interaction, not a replacement peptide bond between those positions. Pauling, Corey and Branson proposed the helical arrangement in their 1951 paper by reasoning from the geometry of small molecules. See Pauling, Corey and Branson, The Structure of Proteins: Two Hydrogen-Bonded Helical Configurations of the Polypeptide Chain, PNAS 37, 205–211 (1951).
Rotating Ball-and-stick model of an alpha helix structure
. Source. New to topics? Read the docs here!
