- Lecturer in Physical Chemistry
- Areas of expertise
- Time-resolved serial crystallography, Transient absorption spectroscopy, X-ray crystallographic methods development, Protein stability
- 1.16 Chemistry Building
- Engineering & Physical Sciences
The relationship between molecular structure and function is driven by dynamics. To fully understand the mechanisms that underpin life it is essential to develop tools able to interrogate dynamics across a range of length and time scales. From ultra-fast processes in single molecules, to complex multistep reactions in the cell. My lab is working towards developing tools to allow researchers to watch molecules undergoing their various functions in real time including time-resolved X-ray crystallography, spectroscopy, and new techniques for X-ray imaging.
Current major projects
- Developing new methods for time-resolved crystallography
- Multimodal data collection for integrated structural biology
- Investigating photo/radiation damage mechanisms in proteins
- Investigating the molecular basis of cataract formation
Detailed research programme
Investigating UV damage mechanisms in the human eye lens protein γ-D crystallin
The human eye lens proteins are extremely stable. To maintain the transparency of the human eye lens, proteins are expressed in the foetal lens prior to lens cell differentiation which involves the removal of cellular machinery. These proteins must, therefore, remain in their soluble and folded state for entirety of human life. However, over the life-course these proteins begin to lose their stability and aggregation occurs leading to the formation of cataract. Cataract is the leading cause of blindness worldwide and presents a major challenge to healthy ageing. We are investigating the structural and dynamic properties that contribute to the stability of this protein and investigating the role of UV in damage mechanisms leading to aggregation.