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Assignment of proton NMR resonances and conformational analysis of the K13CK cystatin‐like peptide
Author(s) -
Samsoen Catherine,
Lebrun Evelyne,
Van Rapenbusch Roland,
Davoust Daniel,
Lalmanach Gilles
Publication year - 1992
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/mrc.1260301014
Subject(s) - chemistry , intramolecular force , peptide , chemical shift , amide , proton nmr , peptide bond , two dimensional nuclear magnetic resonance spectroscopy , nuclear magnetic resonance spectroscopy , crystallography , stereochemistry , proton , cysteine , cyclic peptide , nmr spectra database , nuclear magnetic resonance , spectral line , organic chemistry , biochemistry , physics , quantum mechanics , astronomy , enzyme
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 cis ‐ trans isomerism at the Ala 10 Pro 11 peptide bond.