A common motif in the secondary structure of proteins, the alpha helix (α-helix) 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 (see below). 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.
CITATION STYLE
Chalmers, J. H. (2015). Alpha Helix. In Encyclopedia of Astrobiology (pp. 69–70). Springer Berlin Heidelberg. https://doi.org/10.1007/978-3-662-44185-5_54
Mendeley helps you to discover research relevant for your work.