title: Characterization at atomic resolution of peptide helical structures.
abstract: A survey of literature for the various types of helices experimentally observed in high-resolution 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 alpha-helix, the 3(10)-helix, the fully extended conformation (2(5)-helix) and the beta-bend ribbon spiral. For each of these structures the characteristic phi, psi conformational parameters, n, the number of residues per turn, h, the height per residues and p, the pitch of the helix are described.
authors.affiliation: CNR, Department of Chemistry, University of Napoli, Italy.
authors.forename: E
authors.initials: E
authors.lastname: Benedetti
authors.forename: B
authors.initials: B
authors.lastname: Di Blasio
authors.forename: V
authors.initials: V
authors.lastname: Pavone
authors.forename: C
authors.initials: C
authors.lastname: Pedone
authors.forename: C
authors.initials: C
authors.lastname: Toniolo
authors.forename: M
authors.initials: M
authors.lastname: Crisma
mesh_terms: D008958:Models, Molecular; D011487:Protein Conformation; D014961:X-Ray Diffraction