Interests
Protein misfolding is associated with a wide range of human disorders including Alzheimer’s and Parkinson's diseases, systemic amyloidosis and Motor Neurone Disease. Due to the prevalence of these disorders it is crucial to increase our understanding, at a molecular level, of the mechanisms by which disease-related peptides and proteins aberrantly behave. As the process of amyloid formation results in the population of a highly heterogeneous array of different protein conformers, it is extremely difficult to resolve how specific misfolded protein states evoke detrimental cellular responses. With this challenge in mind, we aim to define these elusive structural attributes using techniques, such as biomolecular NMR and fluorescence microscopy, to relate protein structural characteristics with their influence on cellular trafficking, homeostasis and cell-to-cell transfer processes, factors that are crucial in disease progression.