Mechanical Rigidity of DNA and its Relation to DNA-Protein  Interactions
{'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}
Dr. Austin is studying the sequence dependence of the elastic                   properties of DNA and its implications for specificity in                       protein-DNA interactions.  The goals are ambitious and involve                  the complete integration of physical and biological methodology.                                                                                                Until recently crystallographic data were only available for                    isolated protein or DNA molecules, that is, not docked together                 in a biological complex.  As a result, models for site specific                 protein binding have often had a "lock and key" quality.                        They attempt to understand recognition in terms of a simple                     interaction between rigid and non--allosteric partners.  This                   project will attempt to show that the bending and torsional                     strain stored in DNA upon complexation is of equal importance in                binding specificity.
{'FirstName': 'Robert', 'LastName': 'Austin', 'PI_MID_INIT': 'H', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Robert H Austin', 'EmailAddress': 'austin@princeton.edu', 'NSF_ID': '000296168', 'StartDate': '02/01/1989', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
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{'Code': '114400', 'Text': 'Molecular Biophysics'}
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