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  • Title: Preparation and conformational study of clupeine fragments.
    Author: Bonora GM, Bertanzon F, Toniolo C.
    Journal: Int J Pept Protein Res; 1981 Feb; 17(2):181-8. PubMed ID: 7228496.
    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.
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