Abstract 1237 Development of a Rational Ligand Discovery Method for Dynamic Proteins

Just 20-40% of the human proteome is predicted to be ligandable with current non-covalent small molecule methodology, leading to a large array of biologically important and disease contributing proteins that are inaccessible with small molecules. Dynamic and disordered proteins, in particular, are often passed over as drug targets due to limited structural information and their scarcity of traditional binding pockets. Here, we aim to develop and experimentally validate a computational predictive method, MixMD, to identify promising and previously hidden binding sites for difficult to target protein classes.