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- W2040487568 abstract "The conformation of Naja mossambica mossambica cardiotoxins II and III in aqueous solution, as well as bound to negatively charged dimyristoylphosphatidic acid, has been studied by laser Raman spectroscopy. The conformation of both toxins in solution is distorted anti-parallel β-sheet with no significant amount of α-helix, cardiotoxin II, however, being much more resistant to heat-denaturation. The spectrum of cardiotoxin III with reduced and methylated cysteines shows that the toxin is completely unfolded into the random-coil conformation. Tyrosine 51 is strongly hydrogen-bonded for both native toxins, while tyrosine 22 appears to be hydrogen-bonded only in cardiotoxin III. Upon binding to charged dimyristoylphosphatidic acid, the native conformation of the investigated cardiotoxins, which is tighfly held in space by the presence of the four disulfide bridges, is not affected, but for cardiotoxin III it becomes much more temperature-resistant. On the other hand, a structural change in file flexible conformation of cardiotoxin III with reduced and methylated cysteines occurs upon binding and results in the formation of β-sheet structure. Native and unfolded cardiotoxin III also have drastically different effects on the phospholipid structure. Unfolded cardiotoxin III seems to be able to change its conformation at the interface without any penetration into the bilayer. On the other hand, native cardiotoxins II or III are rather undeformable and penetrate the bilayer so that they cause a marked increase of the phospholipid intramolecular chain disorder." @default.
- W2040487568 created "2016-06-24" @default.
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- W2040487568 date "1982-06-01" @default.
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- W2040487568 title "Conformation of free and phospholipid-bound cardiotoxins from Naja mossambica mossambica by laser Raman spectroscopy" @default.
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- W2040487568 doi "https://doi.org/10.1016/0167-4838(82)90075-9" @default.
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