Cephalopod Hemocyanins:  Structure and Function
{'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}
The aim of the project to understand the structure, assembly,                   and physiological function of a very large multi-subunit                        protein, the hemocyanin of the Pacific octopus, Octopus                         dofleini.  The functional macromolecular assemblage is a                        decamer of very large polypeptide chains, each of mass 3.5 x                    105 daltons.  Each monomer chain is folded into seven                           domains, each of which carries an oxygen binding site.  The                     amino acid sequence of the monomer chain from a c-DNA                           library, is being determined the entire sequence.  Comparison                   of sequences between domains will provide an unusual view of                    protein evolution, since tandem copies of a primitive gene                      are being examined.                                                                                                                                             Individual domains with the intention of determining (or                        groups of domains) will be isolated and attempts will be made                   to correlate differences in oxygen binding function with                        sequences, and to determine what role different domains may                     play in the assembly process.  If it proves possible to                         reassociate subunits from which one or more domains have been                   removed, the oxygen binding will be analyzed to see what                        extent the binding retains to cooperative character observed                    in the native decameric molecule.                                                                                                                               A common theme is many of these observations is the great                       disparty in oxygen binding between the whole decamer and its                    parts.  What is needed are oxygen binding experiments using                     either dimeric structure or decamers in which one or more                       domain types are missing, to probe the role of parts of the                     structure in the functioning of the whole.  It may now be                       possible.  Another aspect of interest is evolution,  how did                    molluscan and arthropod hemocyanins arise and independently                     evolve?  //
[{'FirstName': 'Karen', 'LastName': 'Miller', 'PI_MID_INIT': 'I', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Karen I Miller', 'EmailAddress': 'millerka@ucs.orst.edu', 'NSF_ID': '000461102', 'StartDate': '02/15/1989', 'EndDate': None, 'RoleCode': 'Co-Principal Investigator'}, {'FirstName': 'Kensal', 'LastName': 'Van Holde', 'PI_MID_INIT': 'E', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Kensal E Van Holde', 'EmailAddress': 'vanholdk@ucs.orst.edu', 'NSF_ID': '000341263', 'StartDate': '02/15/1989', 'EndDate': None, 'RoleCode': 'Principal Investigator'}]
{'Name': 'Oregon State University', 'CityName': 'CORVALLIS', 'ZipCode': '973318655', 'PhoneNumber': '5417374933', 'StreetAddress': '1500 SW JEFFERSON AVE', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Oregon', 'StateCode': 'OR', 'CONGRESSDISTRICT': '04', 'CONGRESS_DISTRICT_ORG': 'OR04', 'ORG_UEI_NUM': 'MZ4DYXE1SL98', 'ORG_LGL_BUS_NAME': 'OREGON STATE UNIVERSITY', 'ORG_PRNT_UEI_NUM': None}
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{'Code': '1144', 'Text': 'Molecular Biophysics'}
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