Thermomechanical and Interfacial Behavior of Concentration  Protein Solutions
{'Code': '07020000', 'Directorate': {'Abbreviation': 'ENG', 'LongName': 'Directorate For Engineering'}, 'Division': {'Abbreviation': 'CBET', 'LongName': 'Div Of Chem, Bioeng, Env, & Transp Sys'}}
{'SignBlockName': 'Jeffrey Foltz', 'PO_EMAI': 'jfoltz@nsf.gov', 'PO_PHON': '7032924231'}
Research Summary:  The objective of this research is to develop a               more fundamental understanding of the thermodynamic and mechanical              properties of concentrated protein solutions, including protein gels,           under conditions where both inter- and intra-molecular interactions             are important.  Experimental studies, employing bovine serum albumin            as a model system, will involve both osmotic pressure measurements              and tracer solute partitioning during osmotic equilibrium.  In                  combination, these data can be used to evaluate solution                        non-idealities and the compressive pressure, a parameter used in the            thermodynamic model to characterize the contribution of both inter-             and intra-molecular interactions.  Theoretical analyses of solution             non-idealities will involve application of polymer lattice models, for          example, Flory-Huggins theory, to the concentrated protein solutions.           Inter-molecular attractions and repulsions will be modelled using               McMillan-Mayer solution theory.                                                                                                                                 Potential Impact:  The results from the current study, as well                  as those from future investigations, will have applications in                  the analysis of a variety of protein separation processes in                    which inter- and intra-molecular interactions are thought to be                 important, e.g., protein crystallization and precipitation.                     The thermodynamic data and models will also provide insight                     into the use of liquid-liquid extraction for protein                            separations.  The results from this study can also be used to                   analyze selective protein filtration, the use of membrane                       ultrafiltration to separate proteins of differing molecular                     weight on the basis of size.
{'FirstName': 'Andrew', 'LastName': 'Zydney', 'PI_MID_INIT': 'L', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Andrew L Zydney', 'EmailAddress': 'zydney@engr.psu.edu', 'NSF_ID': '000154295', 'StartDate': '07/01/1987', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'University of Delaware', 'CityName': 'NEWARK', 'ZipCode': '197160099', 'PhoneNumber': '3028312136', 'StreetAddress': '220 HULLIHEN HALL', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Delaware', 'StateCode': 'DE', 'CONGRESSDISTRICT': '00', 'CONGRESS_DISTRICT_ORG': 'DE00', 'ORG_UEI_NUM': 'T72NHKM259N3', 'ORG_LGL_BUS_NAME': 'UNIVERSITY OF DELAWARE', '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'}, {'Code': '9120', 'Text': 'CROSS-DIRECTORATE PROGRAMS'}]
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1987&All=true', 'xml': '8708871.xml'}