Transfer RNA Structure During Protein Synthesis
{'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}
The long term goal of this project is to determine the nature                   of site specific structural and functional interactions of                      transfer RNA (tRNA) with other nucleic acids and proteins                       particularly with regard to the structure found around the                      modified nucleosides.  Site specific heteronuclear enrichment                   of modified nucleosides combined with proton and                                heteronuclear NMR techniques (for the probing of local                          conformations and structure not readily accessible by other                     methods) will be carried out.  A unique E. coli plasmid has                     been constructed into which any chemically synthesized tRNA                     gene can be placed for overproduction of the tRNA in vivo.                      Both 13C-enriched wild type and designed mutant tRNAs with                      site selected nucleoside changes can be produced in quantity                    for analysis of biochemical function and for NMR studies.                                                                                                       The interaction of tRNA with proteins and nucleic acids                         depends upon the tRNA molecule's conformation in solution and                   its specific flexibilities, neither of which are fully                          understood.  A study of tRNA conformation and site specific                     mobility is also important for a comparison of E. coli and                      yeast tRNA structures.  The advantage of NMR over other                         physical techniques in studying macromolecules in solution is                   that signals are obtainable from reporter groups in many                        different parts of the molecules simultaneously.
[{'FirstName': 'Paul', 'LastName': 'Agris', 'PI_MID_INIT': 'F', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Paul F Agris', 'EmailAddress': 'paul.agris@duke.edu', 'NSF_ID': '000591686', 'StartDate': '09/01/1988', 'EndDate': None, 'RoleCode': 'Principal Investigator'}, {'FirstName': 'Hanna', 'LastName': 'Sierzputowska-Gracz', 'PI_MID_INIT': None, 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Hanna Sierzputowska-Gracz', 'EmailAddress': 'hanna_gracz@ncsu.edu', 'NSF_ID': '000399358', 'StartDate': '09/01/1988', 'EndDate': None, 'RoleCode': 'Co-Principal Investigator'}]
{'Name': 'North Carolina State University', 'CityName': 'RALEIGH', 'ZipCode': '276950001', 'PhoneNumber': '9195152444', 'StreetAddress': '2601 WOLF VILLAGE WAY', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'North Carolina', 'StateCode': 'NC', 'CONGRESSDISTRICT': '02', 'CONGRESS_DISTRICT_ORG': 'NC02', 'ORG_UEI_NUM': 'U3NVH931QJJ3', 'ORG_LGL_BUS_NAME': 'NORTH CAROLINA STATE UNIVERSITY', 'ORG_PRNT_UEI_NUM': None}
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[{'Code': '1144', 'Text': 'Molecular Biophysics'}, {'Code': '1164', 'Text': 'MOLECULAR BIOPHYSICS'}, {'Code': '9120', 'Text': 'CROSS-DIRECTORATE PROGRAMS'}, {'Code': '9145', 'Text': 'SPECIAL PROGRAMS-RESERVE'}]
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1988&All=true', 'xml': '8804161.xml'}