Reversed unfolding-refolding process of cobra neurotoxin

Circular dichroism and nuclear magnetic resonance spectroscopies have been used to study the unfolding process of cobrotoxin upon addition of fluoro alcohols/or sodium dodecyl sulfate to its aqueous solution. In each final unfolded state, the protein had its disulfide bonds intact. The unfolding process has been found to be reversible in the case of fluoro alcohol/water mixtures, while no such reversibility was found in the case of sodium dodecyl sulfate. However, when hexafluoro-2-propanol is added to the sodium dodecyl sulfate unfolded protein, refolding is induced. The mechanism of unfolding is discussed in terms of the different interactions which govern the protein conformation in solution.