One of the essential keystones for the existence of life rests in the intricate relationship between biomolecular function, structure, and their dynamics. The biomolecular machines engaging in these indispensable processes possess internal structural dynamics on a wide range of time-scales. It is the relationship or connection between the time-scales of these fundamental biophysical phenomena and the time-scales of biomolecular dynamics that the technique of Nuclear Magnetic Resonance (NMR) spectroscopy is uniquely equipped to explore. NMR is a powerful technique whose observables are time-scale sensitive. Given that the sample is tractable for NMR studies, the system can be explored in solution without chemical modification while maintaining atomic resolution. The focus of our group is to investigate connections between function, structure, and dynamics of biomolecules.
We are interested in studying the role of protein dynamics in molecular recognition such as the interactions of proteins with biomolecules like carbohydrates, nucleic acids, and other proteins, as well as with small molecules and ligands.
NMR Methods Development
The laboratory has expertise in designing NMR experiments. We are interested in improving existing methodologies, designing NMR experiments for the study of biomolecular interactions, as well as the development of associated theory.