title: A new molecular scaffold for the formation of supramolecular peptide double helices: the crystallographic insight.
abstract: [structure: see text]. A series of water-soluble synthetic dipeptides (1-3) with an N-terminally located beta-alanine residue, beta-alanyl-l-valine (1), beta-alanyl-l-isoleucine (2), and beta-alanyl-l-phenylalanine (3), form hydrogen-bonded supramolecular double helices with a pitch length of 1 nm, whereas the C-terminally positioned beta-alanine containing dipeptide (4), l-phenylalanyl-beta-alanine, does not form a supramolecular double helical structure. beta-Ala-Xaa (Xaa = Val/Ile/Phe) can be regarded as a new motif for the formation of supramolecular double helical structures in the solid state.
authors.affiliation: Department of Biological Chemistry, Indian Association for the Cultivation of Science, Jadavpur, Kolkata, India.
authors.forename: Samit
authors.initials: S
authors.lastname: Guha
authors.forename: Michael G B
authors.initials: MG
authors.lastname: Drew
authors.forename: Arindam
authors.initials: A
authors.lastname: Banerjee
mesh_terms: D018360:Crystallography, X-Ray; D004151:Dipeptides / Q000138:chemical synthesis* / Q000737:chemistry*; D006860:Hydrogen Bonding; D008958:Models, Molecular; D017510:Protein Folding; D017433:Protein Structure, Secondary
chemical_list: D004151:Dipeptides