Ray Owens, Ph.D., Head, Oxford Protein Production Facility-UK, Research Complex at Harwell and Professor, Molecular Biology, University of Oxford is a featured presenter at the Eighth Annual Engineering Expression Systems conference at the PEGS Europe Summit in Lisbon, Portugal.
Below, he discusses his interest in protein function, high-throughput expression of recombinant proteins at Oxford, the utility of membrane proteins and technological developments aiding protein analysis.
Protein Function and High-Throughput Expression of Recombinant Proteins
How did you become interested in protein structure and function and what's it like to work on recombinant protein production at Oxford?
Understanding the relationship between protein structure and function has been a theme throughout my career working in both academia and industry and dates back to postdoctoral studies on annexin calcium-binding proteins. In Oxford, I have been involved in establishing a UK national facility for protein production and crystallization. We have developed a range of highly specialized technologies incorporating robotic systems to enable the high-throughput expression, purification and crystallization of recombinant proteins. In partnership with UK academic groups, we are using this technology platform to study a large variety of proteins of biomedical interest.
Why is evaluating multiple membrane proteins and variants a promising avenue for aiding their production for structural and functional studies?
The production of recombinant membrane proteins for structural and functional studies remains technically challenging due to low levels of expression and the inherent instability of many membrane proteins once solubilized in detergents. By exploiting natural sequence variation or using mutagenesis, it has been shown that changing the primary sequence of a membrane protein can have profound effects on both expression and stability.
You'll elaborate on that topic when you give your featured presentation on "Streamlining the Expression Screening of Membrane Proteins" at the Engineering Expression Systems conference. What's the main theme you'd like to convey to your audience?
Combining ligation independent cloning methods with the use of green fluorescent protein as a reporter of folding enables the construction and expression screening of multiple membrane protein/variants to identify candidates suitable in terms of expression and stability for further investment of time and effort.
How do you think your field will evolve in the next 5-10 years?
Technology development continues to drive forward our ability to analyse proteins on different length and time scales. Technical advances in cryo-electron microscopy have opened up the possibility of determining the structure of large protein complexes at high resolution from solution. Super-resolution light microscopy enables the high definition imaging of protein complexes in cells. By integrating these different approaches, it should be possible to improve our understanding of how proteins function as part of supra-molecular complexes in a cellular context.
Ray Owens has extensive experience of the production of recombinant proteins for structural biology both in industry and academia. He obtained his Ph.D. in biochemistry at the University of Cambridge, UK, and has a longstanding interest in protein structure and function. He is currently a Professor of Molecular biology at the University of Oxford and Head of the Oxford Protein Production Facility-UK. This is a National Resource Centre for protein production and crystallisation, based at the Rutherford Appleton Laboratory, near Oxford.
Featured Presentation: Tuesday, 3 November in the Engineering Expression Systems conference: