Probing Surfaces of a Synaptic Receptor
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{'SignBlockName': 'Stacy Springer', 'PO_EMAI': None, 'PO_PHON': None}
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.
{'FirstName': 'Marino', 'LastName': 'Martinez-Carrion', 'PI_MID_INIT': None, 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Marino Martinez-Carrion', 'EmailAddress': None, 'NSF_ID': '000458346', 'StartDate': '02/15/1989', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
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[{'Code': '1188', 'Text': 'SYNAPTIC MECHANISMS'}, {'Code': '1192', 'Text': 'NEURONAL AND GLIAL MECHANISMS'}]
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