Many human proteins have been identified to be intrinsically disordered. Despite these proteins lacking a stable structure, they are still biologically functional. Importantly, many of the disordered proteins are associated with cancer, neurodegenerative disorder, and other human diseases. To understand how proteins operate in our system and develop tools to modulate their activity, uncovering their structural and dynamical properties provides valuable information.
To achieve a better understanding of how disordered proteins function, we use nuclear magnetic resonance (NMR) spectroscopy together with other biophysical and computational techniques (e.g., molecular dynamics simulations) to investigate their structure, dynamics, and interactions with other proteins. The results will improve our understanding of this unique class of protein and provide valuable insight into developing therapies to treat the associated diseases.