Illuminating regulatory mechanisms in the dark proteome

My group focuses on elucidating how post-translational modifications such as phosphorylation regulate 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 region conformations, dynamics, and interactions. I am driven by interesting biological questions but my interests also include NMR methodology and chemical biology approaches.

Proteins are the fundamental molecular machines of life. The ‘dark proteome’ refers to proteins or protein regions that do not have stable 3D structures. These represent about 40% of the human proteome, and they are more often associated with critical cellular functions. I am particularly interested in exploring regulation of transcription factors and kinases, two classes of proteins involved in the development of human disease.