Alpha helix is a common motif in the secondary structure of proteins.
It is a right-handed coiled or spiral conformation, in which every backbone N-H group donates a hydrogen bond to the backbone C=O group of the amino acid four residues earlier ( hydrogen bonding).
This secondary structure is also sometimes called a classic Pauling–Corey–Branson alpha helix. Among types of local structure in proteins, the α-helix is the most regular and the most predictable from sequence, as well as the most prevalent.
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