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Specific assignment of resonances in the 1 H‐nmr spectrum of the polypeptide toxin I from Anemonia sulcata
Author(s) -
Gooley Paul R.,
Norton Raymond S.
Publication year - 1986
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360250308
Subject(s) - chemistry , aqueous solution , sequence (biology) , nmr spectra database , nuclear magnetic resonance spectroscopy , spectral line , molecule , stereochemistry , crystallography , amino acid , toxin , peptide sequence , physics , biochemistry , organic chemistry , quantum mechanics , gene
Abstract The assignment of a large number of resonances in the 300‐MHz 1 H‐nmr spectrum of the polypeptide neurotoxin Anemonia sulcata toxin I is described. The initial identification of spin systems is made using both one‐ and two‐dimensional nmr spectra. The subsequent assignment of these spin systems to specific residues in the molecule is based largely on the observation in two‐dimensional spectra of through‐space connectivities between H α and NH resonances from adjacent residues in the amino acid sequence. Using these techniques, the full spin systems of 22 residues are specifically assigned, together with partial assignments for a further 8. Many of the spin systems from the remaining 16 residues have been defined, although not yet specifically assigned. From the pattern of through‐space connectivities between protons from adjacent residues in the sequence, some inferences may be drawn concerning the secondary structure of this polypeptide in aqueous solution.