title: NMR studies on Ni(II) induced cyclization of a histidine-tagged peptide.
abstract: A linear decapeptide, HGASYQDLGH, was synthesized and used as a model to evaluate the effect of nickel addition upon non-covalent backbone cyclization. The NMR data, obtained for the peptide in the presence of the metal ion, support the existence of predominant folded structures in solution, where the two His residues are maintained close to each other. These results suggest that insertion of even a single His residue at each peptide terminus can be used efficiently to reduce peptide flexibility without any backbone modification.
authors.affiliation: Dipartimento di Biologia Molecolare, Centro per lo Studio Strutturale di Sistemi Biomolecolari, Università di Siena, Italy.
authors.forename: Ottavia
authors.initials: O
authors.lastname: Spiga
authors.forename: Andrea
authors.initials: A
authors.lastname: Bernini
authors.forename: Maria
authors.initials: M
authors.lastname: Scarselli
authors.forename: Arianna
authors.initials: A
authors.lastname: Ciutti
authors.forename: Leonardo
authors.initials: L
authors.lastname: Giovannoni
authors.forename: Franco
authors.initials: F
authors.lastname: Laschi
authors.forename: Luisa
authors.initials: L
authors.lastname: Bracci
authors.forename: Neri
authors.initials: N
authors.lastname: Niccolai
mesh_terms: D000595:Amino Acid Sequence; D003500:Cyclization; D006639:Histidine; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D009532:Nickel / Q000737:chemistry*; D010456:Peptides, Cyclic / Q000737:chemistry*; D017433:Protein Structure, Secondary; D011993:Recombinant Fusion Proteins / Q000737:chemistry*
chemical_list: D010456:Peptides, Cyclic; D011993:Recombinant Fusion Proteins; D006639:Histidine; D009532:Nickel