title: A peptide corresponding to the N-terminal 13 residues of T4 lysozyme forms an alpha-helix.
abstract: Solid-phase methods have been used to synthesize LYS(1-13), a peptide corresponding to the first 13 residues of T4 lysozyme. 2D 1H NMR techniques were used to investigate its solution structure in the presence of SDS micelles. The identification of numerous medium-range NOESY crosspeaks and several slowly exchanging NH protons indicated the presence of an alpha-helical structure. This was confirmed by simulated annealing calculations performed using XPLOR.
authors.affiliation: School of Pharmaceutical Chemistry, Victorian College of Pharmacy, Parkville, Vic., Australia.
authors.forename: M J
authors.initials: MJ
authors.lastname: McLeish
authors.forename: K J
authors.initials: KJ
authors.lastname: Nielsen
authors.forename: J D
authors.initials: JD
authors.lastname: Wade
authors.forename: D J
authors.initials: DJ
authors.lastname: Craik
mesh_terms: D000595:Amino Acid Sequence; D017122:Bacteriophage T4 / Q000201:enzymology*; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D009113:Muramidase / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry*; D017433:Protein Structure, Secondary
chemical_list: D010446:Peptide Fragments; D009113:Muramidase