Proteins are the fundamental molecular machines of life. The ‘dark proteome’ refers to proteins or protein regions that do not have stable 3D structures (disordered regions). These represent about 40% of the human proteome, and they are more often associated with critical cellular functions. For that reason, they are strictly kept in check by post-translational modifications that allow cells to fine tune their function. I am particularly interested in exploring the regulation mechanisms of transcription factors and kinases, two classes of proteins that are tightly regulated to avoid the progression of disease.
My group focuses on elucidating how phosphorylation regulates proteins at the atomic scale. We use solution NMR and other biophysical techniques, as well as chemical biology and cell biology to characterize the effect of phosphorylation on protein disordered regions’ conformations, dynamics, and interactions.