Proteins are molecular machines that bind specific ligands, fold into particular shapes and flex in specific ways in order to function. Nuclear Magnetic Resonance (NMR) is a powerful technique for obtaining information about a protein’s conformation, dynamics and binding partners. However, NMR experiments are often limited in sensitivity and resolution. My research focuses on how to use computational techniques to maximally leverage data obtained in NMR experiments as well as on how to interpret the imprecision of NMR-derived protein structures in terms of protein dynamics. Additionally, my research group is developing bio-informatics based approaches to predict protein flexibility in order to better understand how changes in protein dynamics mediate the evolution of protein function.
