Structure-Function Relationships in Na, K-ATPase
{'Code': '08070400', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'MCB', 'LongName': 'Div Of Molecular and Cellular Bioscience'}}
{'SignBlockName': 'Kamal Shukla', 'PO_EMAI': None, 'PO_PHON': None}
The long-term goal of this research is to understand how ATP                    drives ion transport via the Na,K-Atpase.  A great deal of                      evidence supports a mechanism in which ATP hydrolysis is                        linked to the transport steps through conformational                            transitions induced by substrate and ions.  Despite the fact                    that the enzymatic properties are known in considerable                         detail, little is known about the structures of the major E1                    and E2 states of the Na,K-ATPase, and even less about                           proposed subconformations.  This project consists of                            experiments designed to delineate further the conformational                    states of the enzyme, in particular the interconversions and                    the structural and functional relationships among them.                         Current studies are continued and extended in five major                        areas of structural and kinetic investigations.  (1)                            Determination of structural relationships among enzyme states                   formed by conformationally selective treatments using                           distances measured by Forster energy transfer.  (2)                             Measurement of rates of the conformational steps in the                         reaction cycle with fluorescence stopped-flow.  (3) Labeling                    of the putative ion binding domain with fluorescent                             carbodiimides.  (4) Determination of the function of the IAF                    binding region using antibodies raised to a purified peptide.                   (5) Investigation of species differences in fluorescent                         labeling of Na,K-ATPase by protein sequencing techniques.                       Ion transport across membranes is precisely regulated by                        specific transport systems.  There is a "pump" protein which                    exchanges sodium ions and potassium ions across membranes.                      This plays an important role in regulating cell volume and                      acidity and ion composition.  It is known that the pump                         protein changes shape during ion transport.  It is important                    to the cell to conserve energy during this process.  This                       project will provide new information on the structure of the                    pump and its involvement in energy metabolism.***                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                                //
{'FirstName': 'Joseph', 'LastName': 'Robinson', 'PI_MID_INIT': 'D', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Joseph D Robinson', 'EmailAddress': 'ROBINSOJ@VAX.CS.HSCSYR.EDU', 'NSF_ID': '000249197', 'StartDate': '03/15/1989', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'SUNY, Upstate Medical University', 'CityName': 'SYRACUSE', 'ZipCode': '132102306', 'PhoneNumber': '3154645476', 'StreetAddress': '750 E ADAMS ST', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'New York', 'StateCode': 'NY', 'CONGRESSDISTRICT': '22', 'CONGRESS_DISTRICT_ORG': 'NY22', 'ORG_UEI_NUM': 'HYN3WD58HNN7', 'ORG_LGL_BUS_NAME': 'RESEARCH FOUNDATION FOR THE STATE UNIVERSITY OF NEW YORK, THE', 'ORG_PRNT_UEI_NUM': 'GMZUKXFDJMA9'}
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{'Code': '1144', 'Text': 'Molecular Biophysics'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1988&All=true', 'xml': '8817355.xml'}