Nuclear magnetic resonance (NMR) spectroscopy is a valuable tool for studying the structure and dynamics of biological macromolecules and interactions involved in molecular assemblies. Multidimensional NMR has become the method of choice for determining the structure of small proteins and nucleic acid fragments in solution. With the development of increasingly sophisticated methods, it has become feasible to obtain detailed information about molecular interactions in systems such as drug-DNA, enzyme-substrate, and antibody-antigen complexes.
A major focus of our research has been the development of experiments designed to facilitate the assignment of complex NMR spectra, to obtain distance constraints for use in biomolecular structure determinations, and to measure relaxation rates and other parameters which can be used in studies of the internal dynamics of proteins and nucleic acids.
Studies of the dynamics of biomolecules are mandatory for obtaining a fundamental understanding of the manner in which the molecules function and interact with one another. Through developments in NMR hardware and isotope labeling techniques, it is becoming feasible to use NMR spectroscopy to obtain detailed information on the internal dynamics of biomolecules. With these experimental data and appropriate theoretical tools, it is possible to begin to characterize the dynamic processes present in biomolecules. We are currently studying the intramolecular dynamics of several classes of RNA molecules and a number of different proteins.

Support for trainees is available from a Training Grant in Cardiovascular Research. This training program can be viewed at the following web site: CV Training Grant