Enzyme Structure-Function Relationships
{'Code': '08070400', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'MCB', 'LongName': 'Div Of Molecular and Cellular Bioscience'}}
{'SignBlockName': 'Arthur Kowalsky', 'PO_EMAI': None, 'PO_PHON': None}
Two approaches are proposed to investigate the                                  structure-function relationships responsible for ligand                         binding affinities and catalytic mechanisms of two different                    enzymes, T4 bacteriophage dihydrofolate reductase (T4 DHFR)                     and citrate synthase (CS).  The first will be a                                 crystallographic analysis of the structures of                                  the enzymes, a comparison of these structures in terms of                       ligand affinities and catalytic activity and a further                          comparison with known structures of distantly related or                        mutant forms of the enzymes.  The second approach will                          involve an investigation of the role of electrostatic fields                    in these enzymes.                                                                                                                                               Dihydrofolate reductase catalyzes a reaction in a cyclic                        pathway essential to DNA synthesis.  In particular, it is                       highly susceptible to inhibition by synthetic folate                            compounds, showing high species selectivity.  These compounds                   are of considerable interest for the control of rapidly                         dividing cells.  Citrate synthase catalyzes the condensation                    of oxaloacetate and acetylCoenzyme A to form citrate and                        Coenzyme A.  It is one of a few enzymes capable of directly                     forming a carbon-carbon bond.  It presents an unprecedented                     opportunity to examine an unusual mechanism which probably                      involves sequential conformational changes and electrostatic                    destabilization of substrate.***//
{'FirstName': 'Stephen', 'LastName': 'Remington', 'PI_MID_INIT': 'J', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Stephen J Remington', 'EmailAddress': 'jreming@uoregon.edu', 'NSF_ID': '000434853', 'StartDate': '03/01/1989', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'University of Oregon Eugene', 'CityName': 'EUGENE', 'ZipCode': '974031905', 'PhoneNumber': '5413465131', 'StreetAddress': '1776 E 13TH AVE', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Oregon', 'StateCode': 'OR', 'CONGRESSDISTRICT': '04', 'CONGRESS_DISTRICT_ORG': 'OR04', 'ORG_UEI_NUM': 'Z3FGN9MF92U2', 'ORG_LGL_BUS_NAME': 'UNIVERSITY OF OREGON', 'ORG_PRNT_UEI_NUM': 'Z3FGN9MF92U2'}
{'Name': None, 'CityName': None, 'StateCode': None, 'ZipCode': None, 'StreetAddress': None, 'CountryCode': None, 'CountryName': None, 'StateName': None, 'CountryFlag': None, 'CONGRESSDISTRICT': None, 'CONGRESS_DISTRICT_PERF': '""'}
{'Code': '1144', 'Text': 'Molecular Biophysics'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1988&All=true', 'xml': '8817438.xml'}