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- W2022348654 abstract "A linear decapeptide, HGASYQDLGH, was synthesized and used as a model to evaluate the effect of nickel addition upon non-covalent backbone cyclization. The NMR data, obtained for the peptide in the presence of the metal ion, support the existence of predominant folded structures in solution, where the two His residues are maintained close to each other. These results suggest that insertion of even a single His residue at each peptide terminus can be used efficiently to reduce peptide flexibility without any backbone modification. Copyright © 2002 European Peptide Society and John Wiley & Sons, Ltd." @default.
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- W2022348654 date "2002-01-01" @default.
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- W2022348654 title "NMR studies on Ni(II) induced cyclization of a histidine-tagged peptide" @default.
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- W2022348654 doi "https://doi.org/10.1002/psc.424" @default.
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