Our research focuses on the characterization of dynamic properties of proteins in the context of protein-protein interactions in order to understand how these properties are related to protein function. Specifically, we are interested in a group of enzymes that catalyze the detachment of ubiquitin chains from substrate proteins. Ubiquitin modification has emerged as an important post-translational modification that regulates immune responses and many other cellular processes. The goal is to understand what are the roles of time-dependent conformational properties of both the enzymes and substrates in the substrate recognition process.
We use NMR spectroscopy as the main experimental technique but also combine it with other biochemical and biophysical techniques. Besides the main research direction outlined above, we also are interested in developing NMR methods to improve spectral resolution and sensitivity.