title: CD and NMR determination of the solution structure of a peptide corresponding to T4 lysozyme residues 38-51.
abstract: Solid phase methods have been used to synthesise a peptide corresponding to residues 38-51 of T4 lysozyme. The peptide, LYS(38-51), encompasses helix B in the crystal structure of T4 lysozyme. CD and 1H-NMR analysis showed that the peptide was unstructured in aqueous solution but adopted a helical conformation in the more hydrophobic environment provided by 50% TFE and SDS micelles. The solution structure derived from the NMR data was similar to that of the helix in the X-ray structure, although there was some fraying at the N-terminus.
authors.affiliation: Department of Medicinal Chemistry, Victorian College of Pharmacy, Monash University, Parkville, Vic., Australia.
authors.forename: L V
authors.initials: LV
authors.lastname: Najbar
authors.forename: D J
authors.initials: DJ
authors.lastname: Craik
authors.forename: J D
authors.initials: JD
authors.lastname: Wade
authors.forename: F
authors.initials: F
authors.lastname: Lin
authors.forename: M J
authors.initials: MJ
authors.lastname: McLeish
mesh_terms: D017122:Bacteriophage T4 / Q000201:enzymology*; D002942:Circular Dichroism; D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure; D009113:Muramidase / Q000737:chemistry*; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000737:chemistry*; D012996:Solutions; D014764:Viral Proteins / Q000138:chemical synthesis / Q000737:chemistry
chemical_list: D010446:Peptide Fragments; D012996:Solutions; C094995:T4 lysozyme (38-51); D014764:Viral Proteins; D009113:Muramidase