Preparation and conformational study of clupeine fragments.

G M Bonora, F Bertanzon, C Toniolo

Index: Int. J. Pept. Protein Res. 17(2) , 181-8, (1981)

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Abstract

Fragments of clupeines, YI, YII, and Z of divergent chain length and different amino acid composition were prepared by digestion with thermolysin and a mixture of carboxypeptidases A and B, and their conformational preferences examined as a function of pH, added salts, presence of a helix-supporting solvent, and temperature. All these highly basic oligopeptides adopt an essentially unordered conformation in aqueous solution. 2-Chloroethanol supports in various amounts the onset of the right-handed alpha-helical form in the carboxy-peptidase fragments.