Phase Equilibrium Theory of Aqueous Two-Phase Extraction:   International Collaboration
{'Code': '07020000', 'Directorate': {'Abbreviation': 'ENG', 'LongName': 'Directorate For Engineering'}, 'Division': {'Abbreviation': 'CBET', 'LongName': 'Div Of Chem, Bioeng, Env, & Transp Sys'}}
{'SignBlockName': 'Robert M. Wellek', 'PO_EMAI': None, 'PO_PHON': None}
The aim of this project is the development of a general, comprehensive          theory, based on statistical mechanics, of protein solubility in two-           phase aqueous polymer solutions containing either polyethylene glycol           and dextran or polyethylene glycol and salt.  The objective is to               predict free energies, aqueous phase separations and protein partition          coefficients for a model aqueous polymer two-phase system as a                  function of a number of important parameters:  protein and polymer              concentrations, protein and polymer molecular weights, protein charge,          pH, protein type, polymer type, salt type, ionic strength, temperature          and the binding energy of affinity ligands.  The theory will be                 supported by a series of experiments conducted in international                 collaboration with a world-renown expert in aqueous two phase                   extraction, Prof. Dr. M. R. Kula of the Institute for Enzyme                    Technology in Dusseldorf, Germany.  The experiments will be performed           both in Dr. Kula's laboratory and in the North Carolina State                   University laboratory.                                                                                                                                          Despite the projected importance of aqueous two-phase extractive                techniques for future separations technology, no comprehensive                  theoretical framework exists for predicting protein partitioning in             these systems.  This approach, which is based in statistical                    mechanics, will allow one to investigate the relative importance of             excluded volume effects and electronic interactions and to predict              values for both protein partition coefficients and ion partition                coefficients.  The research should provide insight into the molecular           basis of protein partitioning and yield a useful correlation of                 protein partition coefficients.
{'FirstName': 'Carol', 'LastName': 'Hall', 'PI_MID_INIT': 'K', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Carol K Hall', 'EmailAddress': 'hall@ncsu.edu', 'NSF_ID': '000187003', 'StartDate': '04/01/1988', 'EndDate': None, 'RoleCode': '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}
{'Name': None, 'CityName': None, 'StateCode': None, 'ZipCode': None, 'StreetAddress': None, 'CountryCode': None, 'CountryName': None, 'StateName': None, 'CountryFlag': None, 'CONGRESSDISTRICT': None, 'CONGRESS_DISTRICT_PERF': '""'}
{'Code': '1414', 'Text': 'INTERFAC PROCESSES & THERMODYN'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1987&All=true', 'xml': '8720284.xml'}