ISSN:
0749-1581
Keywords:
K13CK
;
Cystatin-like peptide
;
1H NMR Conformation
;
Chemistry
;
Analytical Chemistry and Spectroscopy
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
Notes:
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 Ala10—Pro11 peptide bond.
Additional Material:
4 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/mrc.1260301014
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