Alpha helices are right-handed due to the specific arrangement of the peptide backbone and the hydrogen bonding pattern that stabilizes their structure. In a right-handed helix, the amino acid side chains project outward, which allows for optimal interactions and minimizes steric clashes. This configuration is energetically favorable, making right-handed helices more common in proteins. Additionally, the chirality of the amino acids contributes to the overall handedness of the helix.
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