Journal article

CONFORMATION OF A PEPTIDE CORRESPONDING TO T4 LYSOZYME RESIDUES-59-81 BY NMR AND CD SPECTROSCOPY

MJ MCLEISH, KJ NIELSEN, LV NAJBAR, JD WADE, F LIN, MB DOUGHTY, DJ CRAIK

BIOCHEMISTRY | AMER CHEMICAL SOC | Published : 1994

Abstract

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..

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