In α-helical folded peptides, the sequential repetition of amino acids generates a chiral layer defined by the amino acid side chains projected outside the amide backbone, and a general exo-helical symmetry model has not been described for the α-helix. Here, the authors introduce the exo-helical symmetry model of the α-helix that results from sequential repetition of amino acid residues and validate the topologies by computational methods and circular dichroism.
- Jose M. Martínez-Parra
- Rebeca Gómez-Ojea
- Julian Bergueiro
