title: The conformation of linear gramicidin is sequence dependent. A monolayer and infrared study.
abstract: A comparative monolayer and infrared study of analogues of gramicidin A containing either tyrosines or naphthylalanines instead of tryptophans indicates that the nature of the aromatic residues influences the favoured conformation of the peptides. Polar residues favour the single stranded IIDL helix while non polar residues favour the double stranded helix. For partly tryptophan to naphthylalanine substituted analogues the positions of the substitutions orientate the favored conformation. The nature of these substitutions may also modify the peptide-lipid interactions.
authors.affiliation: CRBM, CNRS/INSERM, Montpellier, France.
authors.forename: N
authors.initials: N
authors.lastname: Van Mau
authors.forename: B
authors.initials: B
authors.lastname: Bonnet
authors.forename: A
authors.initials: A
authors.lastname: Benayad
authors.forename: F
authors.initials: F
authors.lastname: Heitz
mesh_terms: D000409:Alanine / Q000031:analogs & derivatives / Q000737:chemistry; D000595:Amino Acid Sequence; D006096:Gramicidin / Q000737:chemistry*; D008051:Lipid Bilayers; D008956:Models, Chemical; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D013055:Spectrophotometry, Infrared; D014443:Tyrosine / Q000737:chemistry
chemical_list: D008051:Lipid Bilayers; D006096:Gramicidin; D014443:Tyrosine; C059031:1-naphthylalanine; D000409:Alanine