Over half of drugs currently in use target integral membrane proteins (IMPs) because of the critical roles they play in linking the cell to its environment. However, our knowledge of IMP function and role in disease is limited by the lack of available structures. Although there has been some progress on the experimental and computational frontiers in predicting IMP structure, it remains a formidable challenge. My project is focused on improving computational protein structure prediction of IMPs using paramagnetic restraints. I am developing an experimental approach for collection of accurate paramagnetic data to facilitate our computational protocol. We expect that paramagnetic restraints will guide the prediction to low-energy and experimentally valid conformations and significantly improve IMP structure determination. Overall, we aim to apply our developed protocol to accelerate structure determination of biologically relevant IMPs.