1H Nuclear‐Magnetic‐Resonance Studies of the Conformation of Cardiotoxin VII2 from Naja mossambica mossambica
Open Access
- 1 December 1981
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 120 (3) , 467-475
- https://doi.org/10.1111/j.1432-1033.1981.tb05725.x
Abstract
The membrane toxin VII2 from the venom of N. mossambica mossambica was investigated in aqueous solution by 1-dimensional and 2-dimensional high-resolution NMR techniques at 360 MHz. The spectral characterization included identification of the complete spin systems for several amino acid residues, nuclear Overhauser effect measurements, the use of chemically induced dynamic nuclear polarization and studies of the pH dependence of the NMR spectrum. Data from homologous toxins, in particular direct lytic factor 12B from Haemachatus haemachatus, were used to establish assignments of aromatic and methylproton resonances. A short, triple-stranded fragment of antiparallel .beta. structure was determined which included the residues 23-27, 43-46 and 60-62. The nuclear Overhauser effect measurements indicated close proximity in the protein conformation of the aromatic rings of Trp-14, Tyr-25 and Tyr-59 and the side chain of Ile-46.This publication has 54 references indexed in Scilit:
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