Open AccessSequential Individual Resonance Assignments in the 1 H Nuclear‐Magnetic‐Resonance Spectrum of Cardiotoxin V II 2 from Naja mossambica mossambica
Author(s) -
HOSUR Ramakrishna V.,
WIDER Gerhard,
WÜTHRICH Kurt
Publication year - 1983
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1983.tb07178.x
Subject(s) - cardiotoxin , dipeptide , chemistry , amide , resonance (particle physics) , stereochemistry , side chain , chemical shift , crystallography , amino acid , proton nmr , nuclear magnetic resonance , proton , nuclear magnetic resonance spectroscopy , physics , biochemistry , venom , organic chemistry , particle physics , quantum mechanics , polymer
The assignment of the 1 H nuclear magnetic resonance (NMR) spectrum of cardiotoxin V II 2 from Naja mossambica mossambica is described and documented. The assignments are based entirely on the amino acid sequence and on two‐dimensional NMR experiments at 500 MHz. Individual assignments were obtained at 45 C for the backbone protons of 56 out of the total of 60 amino acid residues, the exceptions being the N‐terminal dipeptide segment Leu‐1–Lys‐2–, Pro‐8 and Pro‐15. Complete assignments of the non‐labile hydrogen atoms of the side chains were obtained for 37 residues, and for Asn‐4 and Asn‐19 the δ amide protons were also identified. For 19 long side chains the individual assignments include only the backbone and C‐β proton resonances; these are Gln‐5, Pro‐9, Pro‐33, Pro‐43, Leu‐47, all three methionines, two arginines and nine lysines. The chemical shifts for the assigned resonances at 45°C are listed for an aqueous solution at pH 3.6. A preliminary interpretation of the sequential connectivity patterns indicates that approximately 30 out of the total of 60 amino acid residues in cardiotoxin V II 2 are in extended, β‐type secondary structures, and there is no indication for the formation of α‐helical structure.