CD and NMR determination of the solution structure of a peptide corresponding to T4 lysozyme residues 38-51.
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.
Najbar
L V
LV
Department of Medicinal Chemistry, Victorian College of Pharmacy, Monash University, Parkville, Vic., Australia.
Craik
D J
DJ
Wade
J D
JD
Lin
F
F
McLeish
M J
MJ
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
D010446:Peptide Fragments; D012996:Solutions; C094995:T4 lysozyme (38-51); D014764:Viral Proteins; D009113:Muramidase