Professor Sheena Radford’s research interests focus on the structural mechanisms of protein folding, misfolding and self-assembly in disease.
Her research is multidisciplinary, combining NMR, MS, CD, fluorescence, hydrogen exchange, stopped flow and ultra-rapid mixing methods and cell biological methods to the problems in hand.
The identification of the folding intermediate that links folding and aggregation energy landscapes.
Identification of the molecular mechanism of prion-like propagation.
The development (with Ashcroft) of MS methods for structural, kinetic and thermodynamic analysis of oligomeric intermediates of amyloid assembly.
Single molecule studies of collapse and conformational change in protein folding (with Brockwell).
The use of simulation methods to provide all-atom models of the structures of non-native states.
These achievements on model proteins can now be applied to understand the aggregation mechanisms of industrially relevant proteins.