1H nuclear-magnetic-resonance studies of the conformation of cardiotoxin VII2 from Naja mossambica mossambica.
The membrane toxin VII2 from the venom of Naja mossambica mossambica was investigated in aqueous solution by one-dimensional and two-dimensional high-resolution nuclear magnetic resonance (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 methyl proton resonances. From these experiments a short, triple-stranded fragment of antiparallel beta structure could be determined, which includes the residues 23-27, 43-46 and 60-62. Furthermore, the nuclear Overhauser effect measurements indicate 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.
D000595:Amino Acid Sequence; D055598:Chemical Phenomena; D002621:Chemistry; D004179:Cobra Cardiotoxin Proteins / Q000302:isolation & purification*; D004546:Elapid Venoms / Q000032:analysis* / Q000302:isolation & purification*; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation
D004179:Cobra Cardiotoxin Proteins; D004546:Elapid Venoms