NMR structure and dynamics of a designed water-soluble transmembrane domain of nicotinic acetylcholine receptor

► We designed a water-soluble analog to the acetylcholine receptor α1 subunit. ► We determined the high-resolution structure of the water-soluble analog by NMR. ► The analog preserved structural features observed in homologous TM domains. ► Photoaffinity labeling identified a relevant anesthetic binding site. ► We affirm the water-solubilization method for high-resolution studies of TM proteins.