Dr Sue Jones

Director of Biomedical Sciences

School of Health Sciences

Protein Folding, Protein purification, Biochemical assays, Molecular biology

My area of research is protein folding and protein mis-folding disorders. During my PhD, I investigated the role of the structure of the bacterial molecular chaperone GroEL on its function. We identified key residues within the large complex molecule that were vital to its folding mechanism. When these residues were mutated, the GroEL molecule lost its ability to form its normal structure and to fold its protein substrates effectively. During my post-doctoral work, I analysed the folding of the protein beta-2-microglobulin (β2m) that forms part of the major histocompatability complex 1 in the immune system of humans. In patients undergoing renal dialysis, the β2m protein levels are elevated as it is not efficiently filtered by the kidneys. This large increase in protein concentration leadmore...

Senior Fellow of the Higher Education Academy (September 2014) (previously FHEA from March 2010) PGCLTHE (post graduate certificate in learning and teaching in higher education) with merit (University of Leeds) December 2009 PhD (University of Birmingham, School of Biological Sciences) July 1998 BSc honours 2.1 (University College of Wales, Aberystwyth, Biochemistry) July 1994

Profile Picture

Latest Publications

  1. Page, M J and Hill, Andrew P. and Kavanagh, Owen and Jones, Sue (2018) Multidimensional Perfectionism and Cortisol Stress Response in Non-Clinical Populations: A Systematic Review and Evaluation. Personality and Individual Differences, 124. pp. 16-24.
  2. Kavanagh, Owen and Jones, Sue (2017) The Pros and Cons of Using Personal Response Systems in an Interactive Scientific Debate. British Journal of Education, Society & Behavioural Science, 19 (2). pp. 1-11.
  3. Erbse, A. and Yifrach, O. and Jones, Susan and Lund, P. A. (1999) Chaperone Activity of a Chimeric GroEL Protein That Can Exist in a Single or Double Ring Form. Journal of Biological Chemistry, 274 (29). pp. 20351-20357.
  4. Jones, Sue and Reader, John S. and Healy, Maria and Capaldi, Andrew P. and Ashcroft, Alison E. and Kalverda, Arnout P. and Smith, D. Alastair and Radford, Sheena E. (2000) Partially Unfolded Species Populated during Equilibrium Denaturation of the β-Sheet Protein Y74W Apo-Pseudoazurin†. Biochemistry, 39 (19). pp. 5672-5682.
  5. Jones, Sue and Manning, James and Kad, Neil M. and Radford, Sheena E. (2003) Amyloid-forming Peptides from β2-Microglobulin—Insights into the Mechanism of Fibril Formation in Vitro. Journal of Molecular Biology, 325 (2). pp. 249-257.
  6. Smith, David P. and Jones, Sue and Serpell, Louise C. and Sunde, Margaret and Radford, Sheena E. (2003) A Systematic Investigation into the Effect of Protein Destabilisation on Beta 2-Microglobulin Amyloid Formation. Journal of Molecular Biology, 330 (5). pp. 943-954.
  7. Jones, Sue and Smith, David P. and Radford, Sheena E. (2003) Role of the N and C-terminal Strands of Beta 2-Microglobulin in Amyloid Formation at Neutral pH. Journal of Molecular Biology, 330 (5). pp. 935-941.
  8. Myers, Sarah L. and Jones, Sue and Jahn, Thomas R. and Morten, Isobel J. and Tennent, Glenys A. and Hewitt, Eric W. and Radford, Sheena E. (2006) A Systematic Study of the Effect of Physiological Factors on β2-Microglobulin Amyloid Formation at Neutral pH†. Biochemistry, 45 (7). pp. 2311-2321.
  9. Shepherd, S. J. and Beggs, C. B. and Jones, Sue (2007) Amino acid partitioning using a Fiedler vector model. European Biophysics Journal, 37 (1). pp. 105-109.
  10. Jones, Susan and Wallington, Emma J. and George, Roger and Lund, Peter A. (1998) An arginine residue (arg101), which is conserved in many GroEL homologues, is required for interactions between the two heptameric rings. Journal of Molecular Biology, 282 (4). pp. 789-800.