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Assignment of proton NMR resonances and conformational analysis of the K13CK cystatin-like peptide

✍ Scribed by Catherine Samsoen; Evelyne Lebrun; Roland Van Rapenbusch; Daniel Davoust; Gilles Lalmanach


Publisher
John Wiley and Sons
Year
1992
Tongue
English
Weight
282 KB
Volume
30
Category
Article
ISSN
0749-1581

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✦ Synopsis


Abstract

The assignments of the proton NMR signals and the conformational analysis of the cystatin‐mimicking peptide K13CK (Lys‐Val‐Gly‐Gly‐Gln‐Val‐Val‐Cys‐Gly‐Ala‐Pro‐Trp‐Lys) in aqueous solution at pH 3.2 have been achieved using two‐dimensional DQF‐COSY, HOHAHA and ROESY nuclear magnetic resonance techniques. The chemical shifts, the magnitudes of the coupling constants, the temperature dependences of the amide protons and the intramolecular NOEs were used to obtain information on the conformation. The NMR spectra of cysteine proteinase inhibitor K13CK demonstrate a cistrans isomerism at the Ala~10~Pro~11~ peptide bond.


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