The 2 major factors that stabilize the alpha helix are the intrachain Hydrogen bonding and the minimization of steric interference between the side chains.
An alpha helix is a kind of secondary structures adapted by proteins. Alpha helices are stabilised by hydrogen bonding. The alpha-helix (-helix), which is a right-hand-coiled or spiral conformation (helix), is a frequent motif in the secondary structure of proteins. Every backbonegroup donates a hydrogen bond to the backbonegroup of the amino acid.
Hydrogen bonds between the "hydrogen" of the amino group in the nth amino acid and the "oxygen" of the carbonyl group in the amino acid are principally responsible for the stability of such structures. Even though a single hydrogen bond has a very low bond strength, the creation of numerous hydrogen bonds stabilises the protein structure sufficiently.
Water soluble proteins, enzymes, antibodies, and other molecules frequently contain alpha helices. The membrane-spanning portion of transmembrane proteins contains alpha helices as well.