Mobility of Proteins Adsorbed at Solid-Liquid Interfaces
{'Code': '07020000', 'Directorate': {'Abbreviation': 'ENG', 'LongName': 'Directorate For Engineering'}, 'Division': {'Abbreviation': 'CBET', 'LongName': 'Div Of Chem, Bioeng, Env, & Transp Sys'}}
{'SignBlockName': 'Fred G. Heineken', 'PO_EMAI': None, 'PO_PHON': None}
The primary objective of this work is to characterize the mobility of           proteins adsorbed at solid-liquid interfaces.  This research                    represents a shift in the emphasis of protein adsorption studies                towards a molecular understanding of the complex behavior of adsorbed           proteins.  It is hoped to quantify the mobility of adsorbed proteins,           characterize the factors governing mobility, identify the mechanism of          adsorbed protein translation, and measure the extent of self-assembly           of proteins into surface islands.  Using a combination of total                 internal reflection fluorescence and fluorescence recovery after                pattern photobleaching, the research will determine protein surface             diffusion coefficients and the fraction of adsorbed proteins that are           mobile.  Mobility will be quantified as a function of shear rate,               surface coverage, and surface residence time in order to identify the           governing factors.                                                                                                                                              Understanding the mobility of adsorbed proteins, as well as the                 related issues of protein structure and organization will aid the               development of effective processes to manufacture protein and                   polypeptide materials.  The utility of these materials is increasing,           not only as pharmaceuticals, but also as novel means of organic                 catalysis, and as the active agent in biosensors for chemical                   analysis.  Protein or polypeptide adsorption to solid surfaces is               inevitable in all processes to manufacture, modify, or                          purify these materials.  This is particularly important to protein              and polypeptide manufacture in that an adsorbed protein layer can               influence the biological activity of the cells it contacts,                     including the genetically engineered microorganisms commonly                    employed in industry.  In addition, the proper function of a                    protein or polypeptide depends on the preservation of the correct               structure.  Adsorption to a solid surface can alter that                        structure.
[{'FirstName': 'Channing', 'LastName': 'Robertson', 'PI_MID_INIT': 'R', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Channing R Robertson', 'EmailAddress': 'crr@Chemeng.stanford.edu', 'NSF_ID': '000446396', 'StartDate': '10/01/1988', 'EndDate': None, 'RoleCode': 'Co-Principal Investigator'}, {'FirstName': 'Alice', 'LastName': 'Gast', 'PI_MID_INIT': 'P', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Alice P Gast', 'EmailAddress': 'gast@mit.edu', 'NSF_ID': '000448808', 'StartDate': '10/01/1988', 'EndDate': None, 'RoleCode': 'Principal Investigator'}]
{'Name': 'Stanford University', 'CityName': 'STANFORD', 'ZipCode': '943052004', 'PhoneNumber': '6507232300', 'StreetAddress': '450 JANE STANFORD WAY', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'California', 'StateCode': 'CA', 'CONGRESSDISTRICT': '16', 'CONGRESS_DISTRICT_ORG': 'CA16', 'ORG_UEI_NUM': 'HJD6G4D6TJY5', 'ORG_LGL_BUS_NAME': 'THE LELAND STANFORD JUNIOR UNIVERSITY', 'ORG_PRNT_UEI_NUM': None}
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[{'Code': '1402', 'Text': 'BIOCHEMICAL & BIOMASS ENG'}, {'Code': '9120', 'Text': 'CROSS-DIRECTORATE PROGRAMS'}]
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1988&All=true', 'xml': '8813517.xml'}