Abstract
Neurotoxin II fromNaja oxiana venom is a short-chain snake curaremimetic neurotoxin containing four disulfide bonds. We obtained13C-15N-labeled neurotoxin II to study its internal dynamics and surface properties with atomic resolution. The recombinant protein has the native spatial structure and is biologically active. The nearly complete assignment of1H,13C and15N resonances for neurotoxin II was obtained by heteronuclear triple-resonance nuclear magnetic resonance spectroscopy. Analysis of the secondary chemical shifts of the1Hα,13Cα,13Cβ and13CO nuclei reveal their strong correlation with the protein secondary structure.
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