Binding Energetics and Dynamic Processes in Protein Dimers
{'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}
The essence of biological specificity resides in the energetics,                dynamics and structural aspects of protein-ligand complexes.  Although a        great deal of emphasis has been placed upon elucidation of the                  structural aspects of proteins, primarily through the use of X-ray              diffraction studies, the understanding of ligand binding and enzyme             catalysis cannot proceed in the absence of knowledge of the energetics          and dynamics of the systems.  During the past decade diverse techniques         such as NMR, hydrogen exchange and fluorescence spectroscopy have               demonstrated that proteins are dynamic molecules.  Theoretical                  treatments such as molecular dynamics calculations have also predicted          motions of some proteins residues.  A picture of the protein molecule           has thus developed which is quite different from the rigid, static              descriptions suggested by earlier X-ray diffraction studies.                    Considerable effort is now being focused on elucidating the functional          significance of these motions to enzyme catalysis and the energetics of         ligand binding.                                                                                                                                                 Dr. Jameson will examine ligand binding and subunit-subunit interactions        in malate dehydrogenase, cytoplasmic malate dehydrogenase and elongation        factor using fluorescence spectroscopy, elevated hydrostatic pressure           and enzyme kinetic measurements.  Fluorescence spectroscopy permits the         determination of lifetimes as a function of environment and rotation            dynamics of tryptophans in proteins.  High pressure techniques are              becoming more applied to biological molecules because of the intrinsic          advantages of the technique compared to temperature effects.
{'FirstName': 'David', 'LastName': 'Jameson', 'PI_MID_INIT': 'M', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'David M Jameson', 'EmailAddress': 'djameson@hawaii.edu', 'NSF_ID': '000269421', 'StartDate': '08/01/1987', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'University of Texas Southwestern Medical Center', 'CityName': 'DALLAS', 'ZipCode': '753907208', 'PhoneNumber': '2146484494', 'StreetAddress': '5323 HARRY HINES BLVD', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Texas', 'StateCode': 'TX', 'CONGRESSDISTRICT': '30', 'CONGRESS_DISTRICT_ORG': 'TX30', 'ORG_UEI_NUM': 'YZJ6DKPM4W63', 'ORG_LGL_BUS_NAME': 'THE UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER', 'ORG_PRNT_UEI_NUM': 'X5NKD2NFF2V3'}
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{'Code': '114400', 'Text': 'Molecular Biophysics'}
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