NMR Studies of Enzyme Conformations
{'Code': '08070400', 'Directorate': {'LongName': 'Direct For Biological Sciences'}, 'Division': {'LongName': 'Div Of Molecular and Cellular Bioscience'}}
{'SignBlockName': 'Arthur Kowalsky'}
The primary goal of this project is the assessment of the magnitude, location and significance of the conformational changes that produce NMR spectral changes upon introduction of point mutations in the active site of Staphylococcal nuclease (Snase). The study will allow investigation of how single site amino acid changes affect the inhibitor-enzyme interaction as well as the conformation of the protein and how the conformational changes induced by amino acid replacement are related to changes in enzyme activity. In addition, there will be continued efforts on the development of novel NMR experiments to probe with more reliability the interactions of interest and on the development of computer aided means of analysing NMR data. The conformation of molecules bound to the active sites of enzymes is of importance in determining how enzymes catalyze reactions, which interactions are important in determining enzyme specificity and in the design of new inhibitors of enzymes. This program is the only one in the Wesleyan Chemistry Department concerned with questions of mutagenesis as well as with determinations of protein structure and function. This allows undergraduate students to partake in a broad and viable research effort.
{'FirstName': 'Philip', 'LastName': 'Bolton', 'EmailAddress': 'pbolton@wesleyan.edu', 'StartDate': '09/01/1988', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'Wesleyan University', 'CityName': 'Middletown', 'ZipCode': '064593208', 'PhoneNumber': '8606853683', 'StreetAddress': '237 HIGH ST', 'CountryName': 'United States', 'StateName': 'Connecticut', 'StateCode': 'CT'}
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