 The observation that a single molecule of the toxin suffices to inhibit channel opening is in agreement with experimental data on the amount of toxin per receptor.Some computational studies of the mechanism of inhibition using normal mode dynamics suggest that a twist-like motion caused by ACh binding may be responsible for pore opening, and that this motion is inhibited by toxin binding.α-Bungarotoxin has played a large role in determining many of the structural details of the nicotinic acetylcholine receptors.