My lab is focused on studying the structures, mechanisms and interactions of aggregating proteins. We are particularly interested in a certain fibre-like structure that is formed by a great variety of proteins called amyloid fibrils. We study amyloid proteins involved in disease, including Alzheimer's disease and motor neuron disease, as well as those that have functions in important biological processes.
The kinds of questions we are looking at include:
1) What are the functions of amyloids and aggregates in different biological processes?
2) What are the structural details of aggregates that have functional and disease-relevant roles?
3) How do other proteins and small molecules affect the aggregation of disease-relevant proteins, and at what stage do they affect aggregation? 4) What sequences are important for aggregation processes, and how can these be interfered with?
5) How do disease mutations affect aggregation or functional behaviour of aggregation-prone proteins?
We studying these topics with a range of structural and biophysical techniques including NMR spectroscopy (both solid-state and solution state), fluorescence-based aggregation assays, electron microscopy.
For more info, check out our webpage at www.morris-lab.com