Sequence-specific assignments in the 1H NMR spectr...[Biochemistry. 1988]

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1: Biochemistry. 1988 May 17;27(10):3568-80.Links

Sequence-specific assignments in the 1H NMR spectrum of the human inflammatory protein C5a.

Zuiderweg ER, Mollison KW, Henkin J, Carter GW.

Pharmaceutical Discovery, Abbott Laboratories, Abbott Park, Illinois 60064.

Full sequence-specific assignments for the 1H 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 Wüthrich et al. [Wüthrich, 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.

PMID: 3408713 [PubMed - indexed for MEDLINE]

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Cited by 2 PubMed Central articles

Secondary structure of complement component C3a anaphylatoxin in solution as determined by NMR spectroscopy: differences between crystal and solution conformations.
Nettesheim DG, Edalji RP, Mollison KW, Greer J, Zuiderweg ER. Proc Natl Acad Sci U S A. 1988 Jul; 85(14):5036-40.

[Proc Natl Acad Sci U S A. 1988]
Identification of receptor-binding residues in the inflammatory complement protein C5a by site-directed mutagenesis.
Mollison KW, Mandecki W, Zuiderweg ER, Fayer L, Fey TA, Krause RA, Conway RG, Miller L, Edalji RP, Shallcross MA. Proc Natl Acad Sci U S A. 1989 Jan; 86(1):292-6.

[Proc Natl Acad Sci U S A. 1989]

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Sequence-specific assignments in the 1H NMR spectrum of the human inflammatory protein C5a.

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Cited by 2 PubMed Central articles

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