Protein Function and Dynamics
{'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}
This research project is designed to a) further characterize                    the internal dynamics of selected proteins, b) focus on                         the effects of viscosity, pressure and temperature on the                       dynamics and function of proteins and c) develop                                fluorescence acquisition and analysis protocols for a more                      realistic and accurate relationship between physical models                     and experimental data.  Dr. Eftink will use the methods of                      multi-frequency phase/modulation fluorometry and solute                         fluorescence quenching reactions to characterize the                            emission of individual tryptophan residues in selected                          proteins.                                                                                                                                                       The dynamic properties of proteins are a matter of                              fundamental importance in the understanding of ligand                           binding, catalysis, cooperative effects, protein-protein                        recognition and other functional aspects of proteins.  It is                    clear that there is an important need to know more than the                     static three-dimensional structure of proteins in order to                      unravel the mysteries of their function.  Molecular-dynamics                    calculations can provide insightful simulations of possible                     events, but these calculations must always be guided and/or                     supported by empirical experimental measures of protein                         dynamics.  Solute quenching and other fluorescence techniques                   have contributed greatly to the present data base regarding                     the fluctuations in proteins on the nanosecond time scale.                      Further development of these fluorescence techniques should                     enhance the ability to relate photophysical kinetic                             models to fluorescence data.***//
{'FirstName': 'Maurice', 'LastName': 'Eftink', 'PI_MID_INIT': 'R', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Maurice R Eftink', 'EmailAddress': 'Eftink@olemiss.edu', 'NSF_ID': '000399163', 'StartDate': '09/01/1988', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'University of Mississippi', 'CityName': 'UNIVERSITY', 'ZipCode': '386779704', 'PhoneNumber': '6629157482', 'StreetAddress': '113 FALKNER', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Mississippi', 'StateCode': 'MS', 'CONGRESSDISTRICT': '01', 'CONGRESS_DISTRICT_ORG': 'MS01', 'ORG_UEI_NUM': 'G1THVER8BNL4', 'ORG_LGL_BUS_NAME': 'THE UNIVERSITY OF MISSISSIPPI', 'ORG_PRNT_UEI_NUM': None}
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[{'Code': '114400', 'Text': 'Molecular Biophysics'}, {'Code': '914500', 'Text': 'SPECIAL PROGRAMS-RESERVE'}]
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