Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

The overall goal of this methodology is to identify multiple phosphorylation of an intrinsically disordered protein by nuclear magnetic resonance spectroscopy using tau protein as a case study. This method can help to answer key question in molecular regulation related to disease such as the impact of the phosphorylation on the protein interaction with its molecular partner. The main advantage of this technique is that we can identify site specific phosphorylation in a disordered protein and link it with structural and functional changes.

This method can provide insight into the function. It can also be applied to other proteins such as the disordered remains of the DNA protein from the aPtc virus The applications of this technique extend toward therapy by development of protein, protein interaction inhibitors. This method will be demonstrated by Clement Danis, Clement Despres, Luiza Bessa, and Hamida Merzougui, the PhD students from our group.