Vibrational Spectroscopy of Biological Macromolecules
{'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}
Vibrational spectroscopy is an important physical tool for                      studying structure.  However, in order to realize its                           full potential, such spectroscopic studies must progress                        beyond the band correlation stage to the use of the rigorous                    methods of normal mode analysis, which permit detailed                          predictions to be made of spectral frequencies and                              intensities associated with a given three-dimensional                           structure.  Dr. Krimm has laid a strong foundation for such                     approaches by refining an empirical vibrational force field                     for the polypeptide chain and applying it to normal mode                        calculations and the analyses of structure in some simple                       polypeptide systems.  He will now extend this approach to a                     number of new systems, including more complex globular                          proteins, as well as develop a more detailed and                                theoretically-based force field from quantum mechanical                         studies.                                                                                                                                                        The determination of the three-dimensional structure of peptides,               polypeptides and proteins continues to be a necessary goal in                   achieving a molecular understanding of their biological                         functioning.  While X-ray diffraction is clearly the most                       powerful technique for obtaining the structure of a large                       molecule at the atomic level, it is not satisfactory for                        studying conformations in non-crystalline systems or under a                    variety of environmental conditions.  The application of                        spectroscopic methods to the study of protein conformation is                   of particular importance, since they can provide equally                        effective ways of probing molecular structure.                                                                                                                  Vibrational spectroscopy has a long history of application to                   structural studies on polypeptides and proteins.  In recent                     years it has become possible to do meaningful normal                            vibration analyses on such molecules and make specific                          predictions of the vibrational frequencies associated with a                    proposed structure.  As a result, much stronger structural                      conclusions can be reached.
{'FirstName': 'Samuel', 'LastName': 'Krimm', 'PI_MID_INIT': None, 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Samuel Krimm', 'EmailAddress': 'skrimm@umich.edu', 'NSF_ID': '000123602', 'StartDate': '01/01/1989', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
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{'Code': '1144', 'Text': 'Molecular Biophysics'}
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