An α-helix is characterized as:

An α-helix is characterized as a right-handed helix. This structure is a common motif in the secondary structure of proteins, defined by its specific hydrogen bonding pattern. In an α-helix, each carbonyl oxygen in a peptide bond forms a hydrogen bond with an amide hydrogen of the peptide bond four residues earlier in the sequence. This pattern of hydrogen bonding stabilizes the helical structure and gives it its right-handed twist as it extends.

The right-handed configuration refers to the direction in which the helix turns. If you were to hold the helix in front of you, a right-handed helix would spiral upward in the clockwise direction—like a standard right-hand corkscrew. This is essential to many protein functions, as the unique shape and properties of the α-helix allow it to fit into various functional roles within proteins. The distinction of the α-helix from other secondary structures like β-pleated sheets further emphasizes its importance in protein architecture.