1ntx

Publication Abstract from PubMed

Sequence-specific assignments are presented for the polypeptide backbone protons and a majority of the amino-acid-side-chain protons of alpha-neurotoxin from Dendroaspis polylepis polylepis, and individual amide proton-exchange rates with the solvent are reported. The secondary structure and the hydrogen-bonding patterns in the regular secondary structure elements are deduced from nuclear Overhauser effects and the sequence locations of the slowly exchanging amide protons. The molecule includes a three-stranded antiparallel beta-sheet, and there are indications that two additional short chain segments are arranged in an antiparallel beta-sheet. These structural elements are similar, but not identical, to either the secondary structure reported for erabutoxin b in single crystals, or the solution structure of cytotoxin CTXIIb from Naja mossambica mossambica.

Secondary structure determination for alpha-neurotoxin from Dendroaspis polylepis polylepis based on sequence-specific 1H-nuclear-magnetic-resonance assignments.,Labhardt AM, Hunziker-Kwik EH, Wuthrich K Eur J Biochem. 1988 Nov 1;177(2):295-305. PMID:2847926^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.