RUI: Spectroscopic Probing of Peptide Binding Calmodulin    Surface
{'Code': '08070400', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'MCB', 'LongName': 'Div Of Molecular and Cellular Bioscience'}}
{'SignBlockName': 'Arthur Kowalsky'}
The goal of this project is to identify and structurally                        characterize the region in calmodulin (CaM) where amphiphilic                   peptides bind in solution.  Structural flexibility and                          conformational adaptation of the CaM molecule in response to                    ligand binding will be studied.  Steady-state and dynamic                       fluorescence spectroscopic techniques will be used.                                                                                                             CaM is an acidic protein, which, in its Ca(II)-complexed form                   can bind and activate several physiologically important                         enzymes.  Some peptides which are capable of forming basic,                     amphiphilic helices, have very high Ca(II)-dependent                            affinities for CaM and compete with enzymes for binding.                        Thus, the CaM-amphiphilic peptide interface provides an                         attractive structural model for studying functionally                           important interactions of CaM with enzymes.
{'FirstName': 'Gautam', 'LastName': 'Sanyal', 'EmailAddress': None, 'StartDate': '09/01/1988', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'Hamilton College', 'CityName': 'Clinton', 'ZipCode': '133231218', 'PhoneNumber': '3158594678', 'StreetAddress': '198 College Hill Rd.', 'CountryName': 'United States', 'StateName': 'New York', 'StateCode': 'NY'}
[{'Code': '1144', 'Text': 'Molecular Biophysics'}, {'Code': '9120', 'Text': 'CROSS-DIRECTORATE PROGRAMS'}]
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1988&All=true', 'xml': '8805082.xml'}