Structure and Function of Troponin and Myosin
{'Code': '08070400', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'MCB', 'LongName': 'Div Of Molecular and Cellular Bioscience'}}
{'SignBlockName': 'Parag R. Chitnis', 'PO_EMAI': None, 'PO_PHON': None}
The goal of the proposed research is to describe the                       molecular mechanisms of calcium regulation of muscle                            contraction.  The experimental approach will be to investigate                  and compare the structural and functional consequences of                       chemical and genetic modifications of troponin subunits and                     myosin light chains from vertebrate and invertebrate muscles.                   The homology of troponin C (TnC) and both classes of myosin                     light chains (MLCs) is a key feature for this comparison, since                 we hope to identify similarities and differences in the                         structures and interactions of these Ca-binding proteins which                  will help in understanding the mechanism of the two regulatory                  systems.  TnC and MLCs will be investigated using the                           complementary techniques of group-specific chemical                             modification, crosslinking, labeling of Ca-binding sites and                    hydrophobic pockets, site-directed mutagenesis and comparative                  sequence analysis.  Modern techniques of preparative and                        analytical HPLC, gas-phase protein and peptide sequencing, and                  computer-assisted structure prediction will be used for                         purifying and characterizing peptides and identifying                           chemically modified amino acids.  The central hypothesis of the                 research is that comparative analyses of structurally related                   but functionally distinct proteins will reveal fundamental                      common mechanism as well as key specific differences which have                 led to functional specialization.
{'FirstName': 'John', 'LastName': 'Collins', 'PI_MID_INIT': 'H', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'John H Collins', 'EmailAddress': 'collins@umbi.umd.edu', 'NSF_ID': '000100469', 'StartDate': '10/01/1988', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'University of Maryland at Baltimore', 'CityName': 'BALTIMORE', 'ZipCode': '212011531', 'PhoneNumber': '4107063559', 'StreetAddress': '220 ARCH ST OFC LEVEL2', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Maryland', 'StateCode': 'MD', 'CONGRESSDISTRICT': '07', 'CONGRESS_DISTRICT_ORG': 'MD07', 'ORG_UEI_NUM': 'Z9CRZKD42ZT1', 'ORG_LGL_BUS_NAME': 'UNIVERSITY OF MARYLAND, BALTIMORE', 'ORG_PRNT_UEI_NUM': None}
{'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=1987&All=true', 'xml': '8716413.xml'}