46 research outputs found
A potentiometric and CD investigation on the conformational properties of poly(L-p-aminophenylalanine) in aqueous solution.
No full textA potentiometric and CD study on the beta-random coil transition of poly-L-tyrosine in aqueous solution.
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Metal complexes of poly(alpha-amino acids). A potentiometric and circular dichroism investigation of Cu(II) complexes of poly(L-lysine), poly(L-ornithine), and poly(L-diaminobutyric acid).
No full textN-substituted poly(α-amino acids). 2. Conformational properties of poly(γ-ethyl N-methyl-L-glutamate) in various solvent mixtures
No full textIntermolecular indole-imidazolium complexes. II. Interaction of a block copolymer (L-tryptophan)n-(gamma-ethyl-DL-glutamate)m with imidazolium hydrochloride and poly(L-histidine hydrochloride).
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Ferric complexes of acetoacetyl derivatives of poly(L-lysine), poly(L-ornithine), and poly(L-diaminobutyric acid). II. Conformational properties in solution. Evidence for a stereospecific complex formation.
No full textInteraction of polypeptides with metal ions
No full textA study has been made of the interaction of Ni(II) and Co (II) ions with the following polypeptides: poly-(L)-lysine), poly-(L-ornithine), poly-(L-diaminobutyric acid) and poly-(L-histidine). It is shown that complexes involving amino nitrogens or deprotonated peptide nitrogens as ligands are formed at several pH values. Deprotonated peptide nitrogens participate in complex formation even in the case of physiological pH values, when a stable chelate system may be formed. When deprotonated peptide nitrogens in matrix backbones are involved in complex formation, no ordered structures is preserved in the complexes regions of a polypeptide. One may conclude from the results obtained that conformational properties of the polypeptides are strictly correlated to complex formation
Metal complexes of poly(α-amino acids): Cu(II) chelates of acetoacetylated poly(L-lysine), poly(L-ornithine), and poly(L-diaminobutyric acid)
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