Dr Arwen Pearson
X-ray crystallography, Structural Biology, Enzymology, Protein dynamics
Research in my group is focussed on understanding how macromolecular structure leads to function. Biological macromolecules are not static and therefore to understand how they work we need to visualise them with high resolution in both space and time. To address this challenge my group are developing a suite of methodologies for time-resolved structure determination.
Current major projects include:- Development of time-resolved X-ray crystallography and SAXS
- Mechanistic enzymology
- ssRNA virus capsid structure, assembly and disassembly
- Using single crystal UV/Vis, Raman and THz spectroscopy to study prote
Research Effort in my group is currently focussed in four areas: 1) on developing novel data collection methodologies that will allow us to carry out fast time-resolved structural studies on standard monochromatic beamlines, 2) developing a library of photocaging chemistries that can be used to simultaneously trigger a reaction in the crystalline state, 3) developing complementary solution phase experiments to probe large scale conformational rearrangements and 4) developing THz time-domain spectroscopy as a tool to probe global dynamic behaviour.
Detailed research programme Close ▲Selected Publications
Timms, N., Windle, C.L., Polyakova, A., Ault, J.R., Trinh, C.H., Pearson, A.R., Nelson, A., Berry, A. (2013) Structural insights into the recovery of aldolase activity in N-acetyl neuraminic acid lyase by the chemical replacement of the catalytically active lysine with the unnatural amino acid ï§-thialysine. ChemBioChem, in press, Cover Article
Ford, R.J., Barker, A.M., Bakker, S.E., Coutts, R.H., Ranson, N.A., Phillips, S.E.V., Pearson, A.R. & Stockley, P.G. (2013) Sequence-specific, RNA-protein interactions overcome electrostatic barriers preventing assembly of Satellite Tobacco Necrosis Virus coat protein. J. Mol. Biol. 425 1050-1064
Owen, R.L., Yorke, B.A. & Pearson, A.R. (2012) X-ray excited optical luminescence of protein crystals: a new tool for studying radiation damage during diffraction data collection. Acta Cryst. D68 505-510
Smith, M.A., Knowles, P.F., McPherson, M.J., Pearson, A.R. (2011) Dissecting the mechanism of oxygen trafficking in a metalloenzyme, Faraday Discussions, 148 269-282.