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• W2016872988 abstract "This paper presents the comparative comprehensive analysis of NMR structural parameters (NOEs, scalar coupling, chemical shifts) of toxin γ, a cardiotoxin isolated from the venom of Naja nigricollis, and three chemical derivatives, i.e. the 2-nitrophenylsulphonyl (NPS)-Trp11, 3-nitro-Try22 and 3-nitro-Tyr51 derivatives. In previous work, the chemical modifications of single side chains have suggested that these aromatic residues, in association with several lysine residues, contributed to the cytotoxicity of toxin γ. Analysis of these results based on the refined solution structure of the toxin has resulted in the proposl of a conserved phospholipid binding site through which cardiotoxins which cardiotoxins are likely to interact with the membrane of target cells. The present work shows that modifications of either the trypthophan residue or the tyrosine residues, which are within or near the proposed binding site, have no influence on the three-dimensional structure of the protein. On the other hand, the proton exchange study of the backbone amides indicates that the structural core of th protein is destabilized in the three derivatives. This corresponds to the decrease of the overall stability of the protein as indicated by the comparative solvent denaturation study of the unmodified toxin γ and the TrpII derivative. More specifically; the dynamics of the three-stranded β sheet, a part of the structural core, are highly perturbated by the chemical modifications. This sheet was previously proposed as a part of the phospholipid binding site of cardiotoxins. The dynamical perturbation of this site appears to be correlated with the decrease in toxicity of the chemical derivatives." @default.
• W2016872988 created "2016-06-24" @default.
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• W2016872988 date "1994-11-01" @default.
• W2016872988 modified "2023-09-27" @default.
• W2016872988 title "Proton NMR studies of the structural and dynamical effect of chemical modification of a single aromatic side-chain in a snake cardiotoxin Relation of the structure of the putative binding site and the cytolitic activity of the toxin" @default.
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• W2016872988 doi "https://doi.org/10.1016/0022-2836(94)90043-4" @default.
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