Events in Physics
Prof. Athene Donald, University of Cambridge
Protein Aggregation
In order for proteins to function properly they need to be in their native, folded state, and not either partially unfolded or aggregated into larger structures. However, many of the diseases of old age are associated with misfolded and aggregated proteins when things have ‘gone wrong’. We are studying the factors that control the _type_ of aggregation, and the kinetics with which the structures form, working with the model proteins insulin and the milk protein beta-lactoglobulin and using a combination of microscopies to characterise the structures.
Based on this work, we are now extending the work to the clinically relevant system of Abeta, the agent thought to lead to senile plaques in Alzheimer's Disease.