[The demonstration of an extramembranous location for the putative amphipathic helix of the acetylcholine receptor].
It has been demonstrated that the lysyl residues at the centers of the potential amphipathic helices of the alpha- and beta-subunits could be readily labeled in native acetylcholine receptor with anionic electrophiles. This result indicates that the regions in the sequences of the alpha- and beta-polypeptides which patterns of hydropathy are those of amphipathic helices are fully exposed on the surface of the native protein and do not span the membrane.
B P
BP
Dwyer
J
J
Kyte
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002462:Cell Membrane / Q000737:chemistry; D002851:Chromatography, High Pressure Liquid / Q000379:methods; D004557:Electric Organ / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D010455:Peptides / Q000032:analysis / Q000737:chemistry; D011950:Receptors, Cholinergic / Q000032:analysis / Q000737:chemistry*; D014101:Torpedo
D000596:Amino Acids; D010455:Peptides; D011950:Receptors, Cholinergic
Dokazatel'stvo vnemembrannogo raspolozheniia predpolagaemoĭ amfipaticheskoĭ spirali atsetilkholinovogo retseptora.