Sequence-Specific Assignments in the1H NMR Spectrum of the Human Inflammatory Protein C5a

Erik R P Zuiderweg, Karl W. Mollison, Jack Henkin, George W. Carter

    Research output: Contribution to journalArticlepeer-review

    21 Scopus citations


    Full sequence-specific assignments for the1H NMR lines of the backbone protons of the human complement factor C5a are described and documented. the results were obtained by largely following the methodology developed by Wiithrich et. al. [Wuthrich, K., Wider, G., Wagner, G., & Braun, W. (1982) J. Mol. Biol. 155, 311]. Assignments for the majority of the amino acid side chain protons were obtained by using a comparison of double- and triple-quantum-filtered two-dimensional correlated experiments together with the analysis of relayed coherence transfer spectra. the assignments provide the basis for the determination of the thus far unknown three-dimensional structure of C5a from nuclear Overhauser enhancement distance constraints.

    Original languageEnglish (US)
    Pages (from-to)3568-3580
    Number of pages13
    Issue number10
    StatePublished - May 1 1988

    ASJC Scopus subject areas

    • Biochemistry


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