A focussed multi-disciplinary research programme, exploring new concepts in biophysics.
The relationship between the structure of a protein and its function is vital to understanding how molecules give rise to biological effects. However, there is an emerging realisation that it is the flexibility and dynamics of proteins that in many cases drives their functional activity. Understanding this relationship is the next step in our understanding of basic life processes
The scientific approach we take is to apply a broad range of high-level biophysical techniques, giving detailed quantitative information that provdes novel insight. The lab has three major research strands described below
We are developing new experimental approaches to rapidly test proteins for their native function, based on accurate detection of their dynamics and flexibility, what we term the 'dynamic profile'. This technology has major industrial applications but also potential for use in a clinical setting.
One of the big questions in enzymology is the role of the motion of the protein, the enzyme dynamics. In particular, what is the role of dynamics in determining enzyme specificity, mechanism and activity. These are challenging questions, but answering them will contribute to enzyme biotechnology, for example improving enzyme (re)design.
Disordered protein biophysics
There is a very deep rooted notion that proteins must adopt very fixed structures and this fixed structure defines the functional abilities of the protein. However, a very high percentage of proteins contain large regions that are structurally disordered, lacking a defined structure as we currently define it. We are particularly interested in 'disorder-mediated-catalysis'; how enzymes that lack a fixed structure are able to catalyse chemical reactions.