Acquisition of a Spectrofluorometer
{'Code': '08080102', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'DBI', 'LongName': 'Div Of Biological Infrastructure'}}
{'SignBlockName': 'Kathie L. Olsen', 'PO_EMAI': None, 'PO_PHON': None}
Funds have been provided for the purchase of a high performance                 static spectrofluorometer for shared use by a group of                          investigators.  The instrument will be used for four different                  projects involving proteins, each of which utilizes fluorescence                as a technique.  Fluorescence intensity measurements will be used               as a means of monitoring such processes as protein-protein and                  protein-nucleic acid interactions, ligand-induced conformational                changes, and accessibility of fluorophors to quencher.                          Measurements of fluorescence anisotropy will also be used to                    study protein associations and conformational changes.                          Fluorescence energy transfer will be employed as a "spectroscopic               ruler" to measure the separation of sites on a protein.  Studies                of the above kinds require an instrument with high sensitivity                  and stability, low background, and capability of providing                      corrected spectra.  The individual projects are concerned with                  the properties and interactions of the Ca2+-binding regulatory                  proteins calmodulin and troponin C, the nature of the catalytic                 site of papain, the characteristics of nucleic acid-unwinding                   proteins, and the properties of the topoismerase enzymes which                  mediate alterations in the geometry of DNA.                                                                                                                     A central goal of molecular biology is to elucidate the structure               of specific molecules and determine how their chemical                          characteristics influence their activity.  One approach is                      fluorescence spectroscopy, which provides data about molecular                  subgroups and molecule-molecule interactions.  This kind of                     information explains biological processes at their most basic                   level.
{'FirstName': 'Robert', 'LastName': 'Steiner', 'PI_MID_INIT': 'F', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Robert F Steiner', 'EmailAddress': None, 'NSF_ID': '000229812', 'StartDate': '09/01/1988', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'University of Maryland Baltimore County', 'CityName': 'BALTIMORE', 'ZipCode': '212500001', 'PhoneNumber': '4104553140', 'StreetAddress': '1000 HILLTOP CIR', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Maryland', 'StateCode': 'MD', 'CONGRESSDISTRICT': '07', 'CONGRESS_DISTRICT_ORG': 'MD07', 'ORG_UEI_NUM': 'RNKYWXURFRL5', 'ORG_LGL_BUS_NAME': 'UNIVERSITY OF MARYLAND BALTIMORE COUNTY', 'ORG_PRNT_UEI_NUM': 'KMGEN62NKEM9'}
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{'Code': '1108', 'Text': 'INSTRUMENTAT & INSTRUMENT DEVP'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1987&All=true', 'xml': '8703363.xml'}