Active-Site Structures of ATP-Utilizing Enzymes
{'Code': '08070400', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'MCB', 'LongName': 'Div Of Molecular and Cellular Bioscience'}}
{'SignBlockName': 'Arthur Kowalsky', 'PO_EMAI': None, 'PO_PHON': None}
Understanding the catalytic activity of ATP-utilizing enzymes                   on a molecular basis requires knowledge of the structures of                    the reactants and products bound at he active sites of these                    enzymes.  Dr. Rao's goal is to establish the active-site                        structures of three classes of enzymes, phosphory1 transfer,                    nucleotidy1 transfer and pyrophosphory1 transfer by using NMR                   spectroscopy which is one of the few techniques available for                   structural investigations in liquids.                                                                                                                           This is an excellent, well-crafted proposal by a very                           creative scientist.  Dr. Rao has made impressive                                contributions to cleaning up the interpretation of metal-ion                    induced relaxation of substrate molecules in the active site                    of ATP-utilizing enzymes.  This project represents                              significant and important extensions of the ongoing research.
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{'Code': '1144', 'Text': 'Molecular Biophysics'}
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