The study of protein dynamics and unfolding is key to understanding the basis of misfolding and aggregational diseases such as type II diabetes, α1-antrypsin deficiency, Parkinsons’ disease and Alzheimers' disease. Common structural biology techniques, such as x-ray crystallography and cryo electron microscopy often require large quantities of high purity sample and can only capture major structural ensembles. Mass spectrometry coupled to ion mobility (IM-MS) is positioned as an ideal technique to study protein dynamics and unfolding as it allows the separation of ions based on mass, charge and conformation from low concentrations of heterogenous solutions. In this thesis I present new techniques, instrumentation and computational workflows relating to IM-MS and how these techniques can be applied to protein systems involved in misfolding and aggregational diseases
