Enzyme Design and Catalytic Function for Production of NovelMaterials
{'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}
This proposal describes a comprehensive program aimed at                        developing new methods for the production of speciality                         biochemicals and advanced biomaterials.  These materials will be                formed by reversing the normal hydrolytic action of two proteases.              These proteases will be modified to alter their selectivity and to              enhance their stability under reaction conditions.  Trypsin or                  chymotrypsin specificity will be altered by several techniques;                 site-directed mutagenesis, screening for mutants which produce                  enzymes with the ability to act on the substrates of interest,                  refolding partially denatured enzyme around novel substrates and a              new approach which will permit the insertion of synthetic amino                 acids at the active site of the enzyme.  Cathepsin C will be                    modified by a refolding procedure, and immobilized by a variety of              techniques.                                                                                                                                                     Methods for enhancing the reversal of the hydrolytic reaction for               dipeptide and oligomer synthesis with non-natural amino acids will              be developed.  These include the use of non-aqueous solvents (both              water-miscible and immiscible) to increase substrate solubility                 and the use of directed methods for enzyme immobilization to                    enhance enzyme stability under reaction conditions.  Changes in                 enzyme conformation induced by non-aqueous solvents and by                      immobilization will be probed by several techniques, including                  EPR.
{'FirstName': 'Harvey', 'LastName': 'Blanch', 'PI_MID_INIT': 'W', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Harvey W Blanch', 'EmailAddress': 'blanch@berkeley.edu', 'NSF_ID': '000199778', 'StartDate': '08/01/1988', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'University of California-Berkeley', 'CityName': 'BERKELEY', 'ZipCode': '947101749', 'PhoneNumber': '5106433891', 'StreetAddress': '1608 4TH ST STE 201', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'California', 'StateCode': 'CA', 'CONGRESSDISTRICT': '12', 'CONGRESS_DISTRICT_ORG': 'CA12', 'ORG_UEI_NUM': 'GS3YEVSS12N6', 'ORG_LGL_BUS_NAME': 'REGENTS OF THE UNIVERSITY OF CALIFORNIA, THE', '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': '1491', 'Text': 'Cellular & Biochem Engineering'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1988&All=true', 'xml': '8807179.xml'}