Probing Surfaces of a Synaptic Receptor

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The nicotinic acetylcholine receptor (AcChR) is a transmembranous protein whose amino acid sequence is known and organized in an unknown manner from four different polypeptide subunits. Although several organizational models regarding the folding of each subunit based on theoretical calculations have been published, the level of organization remains largely as speculative suggestions. Because there is no hope of obtaining, in the near future, detailed structural atomic coordinates of the receptor in the cell membrane, the research alternatives are to map exposed elements at specific sites (external or internal) of each subunit of the AcChR in membranes. Electric tissue of the electric ray Torpedo californica AcChR will be used to develop markers for detecting the cytoplasmic site and to determine whether the environment of one particular region containing an amino acid (cysteine) that has been highly conserved in the evolution of all species is sensitive to changes in other components of the cell membrane besides the AcChR.