Protein dynamics and structure are intimately related to health and disease. My research aims to understand both the architecture and dynamics of proteins in relation to function and disease. To this end it is vital to achieve a systematic description of protein systems. This can only be acheived by using a combination of biophysical techniques. Including, but not limited to, high resolution Nuclear Magnetic Resonance (NMR), X-ray diffraction (XRD) and native mass spectrometry (MS). Such combinations may elucidate tertiary (XRD) and quaternary (MS) structure along with vital dynamical properties (NMR). I benefit from the extensive experience in NMR and XRD from my two supervisors, Andrew Baldwin (Dept. of Physical and Theoretical Chemistry) and Robert Gilbert (The Division of Structural Biology). Our interdisciplinary approach is used to study three particular protein systems; Small Heat Shock protein chaperone function, Glucocerebrosidase in relation to Gaucher's and Parkinson's disease, and terminal uridyl transferases in the cancer Lin28/Let7 pathway.