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Characterization at atomic resolution of peptide helical structures

A survey of literature for the various types of helices experimentally observed in highresolution single crystal x‐ray diffraction analyses of peptides has allowed to determine accurate conformational and helical parameters for the various secondary structures such as the α‐helix, the 310‐helix, the fully extended conformation (25‐helix) and the β‐bend ribbon spiral. For each of these structures the characteristic ϕ, ψ conformational parameters, n, the number of residues per turn, h, the height per residues and p, the pitch of the helix are described.