Low Temperature Trapping of Intermediates in Enzyme-        Catalyzed Reactions
{'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}
This research involves a combination of method development for                  the acquisition of structural information concerning enzyme-                    substrate or enzyme-inhibitor complexes, and application to the                 study of slow-binding transition-state analog inhibitors, early                 events in protease catalysis and intermediates in glycosidase                   catalysis.  The focus of the investigation is on the                            application of attenuated total reflectance (ATR) Fourier                       transfer infrared spectroscopy to study enzyme-substrate                        intermediates, stabilized at low temperatures, and enzyme-                      inhibitor complexes, and the use of immobilized enzymes and                     stopped-flow kinetics in cryoenzymology studies.  FT-IR has the                 potential to reveal not only new bonds formed in enzyme-ligand                  complexes, but also bond deformations and polarization.                                                                                                         The importance of enzymes in numerous areas of science,                         medicine and industry needs no elaboration.  Recent                             developments in molecular biology and biotechnology have led to                 a greatly increased interest in all aspects of enzymology.  A                   major problem in determining the details of an enzyme.                          Catalytic mechanism is the short lifetime of enzyme - substrate                 complexes and intermediates, making it particularly difficult                   to obtain structural information.  The lifetimes of normal                      transient species can be significantly increased at sintably                    low temperatures.  The development of some methods which should                 facilitate the acquisition of structural data are underway                      here.
{'FirstName': 'Anthony', 'LastName': 'Fink', 'PI_MID_INIT': 'L', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Anthony L Fink', 'EmailAddress': 'enzyme@cats.ucsc.edu', 'NSF_ID': '000310855', 'StartDate': '07/15/1988', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'University of California-Santa Cruz', 'CityName': 'SANTA CRUZ', 'ZipCode': '950641077', 'PhoneNumber': '8314595278', 'StreetAddress': '1156 HIGH ST', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'California', 'StateCode': 'CA', 'CONGRESSDISTRICT': '19', 'CONGRESS_DISTRICT_ORG': 'CA19', 'ORG_UEI_NUM': 'VXUFPE4MCZH5', 'ORG_LGL_BUS_NAME': 'UNIVERSITY OF CALIFORNIA SANTA CRUZ', 'ORG_PRNT_UEI_NUM': None}
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{'Code': '114400', 'Text': 'Molecular Biophysics'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1988&All=true', 'xml': '8810144.xml'}