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. It can be conjugated to a fluorophore or enzyme for immunohistochemical staining of fixed tissues and visualization via light or fluorescence microscopy. This application enables morphological characterization of the neuromuscular junctions.