Conformation of a peptide corresponding to T4 lysozyme residues 59-81 by NMR and CD spectroscopy.
The conformation, in solution, of a peptide corresponding to residues 59-81 from T4 lysozyme [LYS(59-81)] has been determined by 1H NMR and CD spectroscopy. This peptide spans the region corresponding to helix C in the crystal structure of T4 lysozyme. Secondary structure predictions indicated that the peptide would possibly be helical in an aqueous environment, but in a more hydrophobic environment the peptide would certainly adopt a helical conformation. This prediction was confirmed by the far-UV CD and NMR studies, which showed the peptide to be relatively unstructured in aqueous solution and significantly helical in the presence of either TFE or SDS micelles, although the 1H NMR results did give some indication of the presence of nascent helix in aqueous solution. For LYS(59-81), in TFE, the three-dimensional structure derived from the NMR data showed that the helix had a more pronounced curvature than the gradual bend observed in the crystal structure.
McLeish
M J
MJ
School of Pharmaceutical Chemistry, Victorian College of Pharmacy, Monash University, Parkville, Australia.
Nielsen
K J
KJ
Najbar
L V
LV
Wade
J D
JD
Lin
F
F
Doughty
M B
MB
Craik
D J
DJ
D000595:Amino Acid Sequence; D017122:Bacteriophage T4 / Q000201:enzymology; D002851:Chromatography, High Pressure Liquid; D002942:Circular Dichroism; D007202:Indicators and Reagents; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009113:Muramidase / Q000737:chemistry*; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary
D007202:Indicators and Reagents; D010446:Peptide Fragments; D009113:Muramidase