Helvetica Chimica Acta · 1987 · 75 citations · 19 references
Life SciencesBiochemistryMedicinal ChemistryMolecular ImmunologyStructural BiochemistryStructural BiologyMagnetic Resonance SpectroscopyPeptide AnalysisPeptide ChemistryPeptide IdentificationConfiguration Determination By Nuclear Magnetic Resonance SpectroscopyMagnetic Resonance Spectroscopy Of BiomoleculesPeptide Structure Analysis
Abstract The constitution of the nonadecapeptide Ro 09–0198 ( 1 ) has been established by homonuclear two‐dimensional NMR spectroscopy. The peptide contains three sulfide bridges and a bridge formed from the side chain of a lysine residue (lysinoalanine moiety). Only the composition was known before, thus the complete sequencing and the elucidation of the bridges had to be performed. Of special importance was the application of the RELAYED‐NOESY experiment. This technique was improved by the introduction of a double‐quantum filter to reduce the tailing around the diagonal. The resulting sequence of 1 exhibits a surprizing analogy of this immunopotentiating peptide to the ACE inhibitor ancovenin.
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NMR with Proteins and Nucleic Acids
Kurt Wüthrich · Europhysics news · 1986 · 8K citations
Investigation of exchange processes by two-dimensional NMR spectroscopy
J. Jeener, Beat H. Meier, P. Bachmann et al. · The Journal of Chemical Physics · 1979 · 4.8K citations
Natural Sciences, Chemistry, Physics +17