Biophysical Properties of the Bacteriophage T4 Capsid       Protein
{'Code': '08070400', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'MCB', 'LongName': 'Div Of Molecular and Cellular Bioscience'}}
{'SignBlockName': 'Marcia Steinberg', 'PO_EMAI': None, 'PO_PHON': None}
Regulation of the size and shape of subcellular components is                   a major problem faced by all cells.  Ribosomes, muscle thick                    filaments and centrioles have relatively fixed dimensions                       while other components such as cytoskeletal networks have                       fixed dimensions only at certain times in the cell cycle.                       Regulation of the bacteriophage T4 even head length may be                      considered a prototype for systematically exploring the                         molecular mechanisms underlying this problem, primarily                         because of the extremely well defined and versatile genetics                    available.  Furthermore, much is also known of the biophysics                   of the architecture, and the biochemistry of the major capsid                   protein.  There are two models for head length regulation,                      the vernier and the kinetic models.  Each mechanism will be                     tested to determine the role of the major head protein in                       length determination.  In an attempt to establish a set of                      rules defining the types of amino acid changes in the petite                    giant, ptg and petite, pt mutants, the investigator will                        select site directed mutations at additional ptg site.  It is                   possible that pt mutations in the major capsid protein gp 23                    may increase the "intrinsic curvature" of this protein and                      hence produce shorter than normal capsids.  These experiments                   hopefully will generate conclusive results.  Attempts will be                   made to crystalize gp 23.  The past work conducted by this                      investigator, although in a different area, was excellent.                      Dr. Eiserling is certainly capable of carrying out this work                    and the program recommends support with a high priority.
{'FirstName': 'Frederick', 'LastName': 'Eiserling', 'PI_MID_INIT': 'A', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Frederick A Eiserling', 'EmailAddress': 'frede@college.ucla.edu', 'NSF_ID': '000464452', 'StartDate': '07/15/1987', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'University of California-Los Angeles', 'CityName': 'LOS ANGELES', 'ZipCode': '900244200', 'PhoneNumber': '3107940102', 'StreetAddress': '10889 WILSHIRE BLVD STE 700', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'California', 'StateCode': 'CA', 'CONGRESSDISTRICT': '36', 'CONGRESS_DISTRICT_ORG': 'CA36', 'ORG_UEI_NUM': 'RN64EPNH8JC6', 'ORG_LGL_BUS_NAME': 'UNIVERSITY OF CALIFORNIA, LOS ANGELES', 'ORG_PRNT_UEI_NUM': None}
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{'Code': '1144', 'Text': 'Molecular Biophysics'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1987&All=true', 'xml': '8705427.xml'}