title: Spatial structure of the M2 transmembrane segment of the nicotinic acetylcholine receptor alpha-subunit.
abstract: A synthetic peptide corresponding to the transmembrane segment M2 (residues 236-267) of the alpha-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 alpha-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.
authors.affiliation: Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.
authors.forename: V S
authors.initials: VS
authors.lastname: Pashkov
authors.forename: I V
authors.initials: IV
authors.lastname: Maslennikov
authors.forename: L D
authors.initials: LD
authors.lastname: Tchikin
authors.forename: R G
authors.initials: RG
authors.lastname: Efremov
authors.forename: V T
authors.initials: VT
authors.lastname: Ivanov
authors.forename: A S
authors.initials: AS
authors.lastname: Arseniev
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002725:Chloroform / Q000737:chemistry; D007473:Ion Channels / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D000432:Methanol / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011978:Receptors, Nicotinic / Q000737:chemistry*; D012984:Software; D014101:Torpedo / Q000378:metabolism
chemical_list: D007473:Ion Channels; D011978:Receptors, Nicotinic; D002725:Chloroform; D000432:Methanol