Assistant Professor, research focussed

Email:

Phone: 024 765 22568

Office: B142

Research Clusters

Cells & Development

Microbiology & Infectious Disease

Neurosciences

Quantitative, Systems & Engineering Biology

Warwick Centres & Spotlights

WISBIC centre

Opportunities in the group

I welcome undergraduate, MBiol., masters and PhD students into our group for their research projects. I lecture undergraduates on LF206 and BS122.

Research/Teaching Interests

I’m a biochemist with a broad background of biological techniques that can be used to help us understand more about how proteins interact with, and respond to, signals from both inside and outside of the cell. I like to look at the molecular level to understand the mechanisms of these interactions, how they change a protein’s shape, or change how one protein can interact with another. By understanding these details, we learn how proteins function, and why they fail if a gene mutation stops the protein behaving normally. We can also use the information to develop targeted drugs to either enhance or block the protein, according to need. As I like a challenge, I spend most of my time working on membrane proteins.

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Research: Technical Summary

I work on gated ion channels and secondary transporters, using techniques that will enhance our understanding of their structure and function. My main goal is to acquire high resolution 3D structures, using either single particle Cryo-EM or X-ray crystallography. We look to capture as many different states as we can, to help us understand the dynamics of the proteins’ movements when carrying out their function. We support these structural data with a range of biophysical studies, including transport assays, Mass spectroscopy, microscale thermophoresis, binding assays, thermostability assays. My current work is on Prof. Nick Dale’s Leverhulme grant, continuing to look at carbon dioxide sensitive proteins. With this, I have the pleasure of working with physiologists that can look at the effects of mutations and changes in PCO₂ at a cellular level, to complement our structural data too, increasing our understanding of how the proteins function in their natural environment.