Dr Lee Byrne joined Canterbury Christ Church University following a Senior Lectureship at the University of Worcester. His research interests focus on understanding how proteins work at the molecular level and how their three dimensional structures can affect their cellular functions. During his career he has studied proteins involved in disulphide bond formation and the processes involved in prion formation and maintenance in yeast. Dr Byrne obtained his PhD at the University of Kent, where he characterised several protein folding catalysts involved in disulphide bond formation in the yeast Saccharomyces cerevisiae. Following his PhD studies, he was a post-doctoral fellow at St Jude Children’s Research Hospital in Memphis Tennessee, where he investigated the action of anticancer drugs on DNA replication. On returning to the University of Kent as a postdoctoral researcher and research fellow in mathematical biology, Dr Byrne investigated prion propagation in budding yeast, confirming that cell division is necessary to cure yeast cells of prions and developed a statistical model to predict the number of infectious prion particles (propagons) within a typical yeast cell. Dr Byrne then spent his final postdoctoral position investigating the dynamic motions inherent within the protein folding catalyst, protein disulphide isomerase using NMR spectroscopy and his current research interests are still in both the yeast prion and protein folding areas.
In addition to his love of proteins, Dr Byrne has a passion for teaching and teaches primarily on the chemistry and biochemistry-based modules at Canterbury Christ Church University.
Research and knowledge exchange
Current Research areas include:
- Prion propagation in the budding yeast Saccharomyces cerevisiae
- Dynamics and structure of the protein folding catalyst protein disulphide isomerase (PDI)
Teaching and subject expertise
Modules currently taught:
Core Science (Chemistry and Biochemistry)
Environmental and Organic Chemistry
Dr Byrne is a member of the Biochemical Society
Publications and research outputs
- Wallis, A.K., Sidhu A., Byrne, L.J., Howard, M.J., Ruddock, L.W., Williamson, R.A. and Freedman R.B. (2009) The ligand-binding b’ domain of human PDI mediates homo-dimerization. Protein Science, 18, 2569-2577.
- Byrne, L.J., Sidhu, A., Wallis, A.K., Ruddock L.W., Freedman, R.B., Howard, M.J. and Williamson R.A. (2009) Mapping of the ligand binding site on the b’ domain of human PDI; interaction with peptide ligands and the x-linker region. Biochemical Journal, 423, 209-217.
- Byrne, L.J., Cole, D.J., Cox, B.S., Ridout, M.S., Morgan, B.J.T. and Tuite, M.F. (2009) The number and transmission of [PSI+] prion seeds (propagons) in the Yeast Saccharomyces cerevisiae. PLoS ONE, 4(3):e4670. doi:10.1371/journal.pone.0004670
- Byrne, L.J., Cox, B.S., Cole, D.J., Ridout, M.S., Morgan, B.J.T. and Tuite, M.F. (2007) Cell division is essential for elimination of the yeast [PSI+] prion by guanidine hydrochloride. Proceedings of the National Academy of Sciences of the United States of America 104, 11688-11693.
- Cole, D.J., Ridout, M.S., Morgan, B.J.T., Byrne, L.J. and Tuite, M.F. (2007) Approximations for expected generation number. Biometrics 63 1023-1030.
- Cox, B.S., Byrne, L.J. and Tuite, M.F. (2007) Prion Stability. Prion 1 170-178.