Spatial structure of the M2 transmembrane segment of the nicotinic acetylcholine receptor α‐subunit

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Abstract
A synthetic peptide corresponding to the transmembrane segment M2 (residues 236–267) of the α‐subunit of the nicotinic acetylcholine receptor from Torpedo californica has been studied by two dimensional 1H‐NMR spectroscopy in a chloroform‐methanol (1:1) mixture containing 0.1 M LiClO4. Reconstruction of the spatial structure of M2 from the NMR data resulted in an α‐helix formed by residues 241–263. Distribution of the molecular hydrophobicity potential on the helix surface is very similar to that in five‐helix bundles of proteins with a known three dimensional structure: two hydrophilic bands located on the opposite helix sides separated by strong hydrophobic zones.