The helical (commonly right-handed) form present in many proteins, deduced by Pauling and Corey from x-ray diffraction studies of proteins such as alpha-keratin; the helix is stabilised by hydrogen bonds between, e.g., ==C==O and HN== groups (symbolised by the centre dot in ==CO-HN==) of different eupeptide bonds. In a true a helix, there are 3.6 amino acid residues per turn of the helix.
collagen helix, an extended left-handed helix resulting from the high levels of glycine, l-proline, and l-hydroxyproline present in the collagens. There are 3.3 amino acids per turn of the helix. Three of those left-handed helices form a triple superhelix that is right-handed.