NMR studies on Ni(II) induced cyclization of a histidine-tagged peptide.
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.
Spiga
Ottavia
O
Dipartimento di Biologia Molecolare, Centro per lo Studio Strutturale di Sistemi Biomolecolari, Università di Siena, Italy.
Bernini
Andrea
A
Scarselli
Maria
M
Ciutti
Arianna
A
Giovannoni
Leonardo
L
Laschi
Franco
F
Bracci
Luisa
L
Niccolai
Neri
N
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*
D010456:Peptides, Cyclic; D011993:Recombinant Fusion Proteins; D006639:Histidine; D009532:Nickel