Nuclear Magnetic Resonance and its application to the structural studies of biologically important macromolecules.

Nuclear Magnetic Resonance offers unparalleled opportunities to examine not only the structure of biologically important macromolecules (proteins, nucleic acids, carbohydrates), but the interaction of these macromolecules with other molecules that affect their function. Rational design of new drugs based on the information returned can be an important aide in combating disease. We develop new NMR-based methods that extend the range of applicability of NMR both in terms of the size of systems that can be studied, and the environment in which they can be studied.

Our lab has been developing NMR methodology that can define the relative orientation of parts of biomolecular complexes using a combination of liquid crystal media and very high field magnets. The National Institutes of Health has selected the University of Georgia as a host site for a regional high field NMR facility, partly so that these methodologies can be exploited. The methodologies are being applied to rapid determination of backbone structures of proteins as part of a structural genomics project, and they are being used as a basis for a rational drug design strategy in which the preferred orientations of carbohydrate ligands in protein binding sites are determined.  The latter project has become an important element of a new NIH funded Research Resource for Integrated Glycotechnology that involves the cooperative efforts of five senior investigators of the Complex Carbohydrate Research Center of the University of Georgia.

Georgia, through organizations such as the Georgia Research Alliance has been willing to invest in new technologies, and in the educational structure that assures the development of future technologies. There is real excitement in working in a community that wants to grow and is willing to make the commitment necessary to make this happen.