Reversed unfolding-refolding process of cobra neurotoxin

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Abstract
Circular dichroism and NMR spectroscopies were used to study the unfolding process of cobratoxin on addition of fluoro alcohols and/or sodium dodecylsulfate to its aqueous solution. In each final unfolded state, the protein had its disulfide bonds intact. The unfolding process was reversible in the case of fluoroalcohol/water mixtures; no reversibility was found in the case of sodium dodecylsulfate. When hexafluoro-23-propanol was added to the sodium dodecylsulfate unfolded protein, refolding was induced. The mechanism of unfolding was discussed in terms of the different interactions which governed the protein conformation in solution.