Ren Dobson in lab high-res

ProfessorRenwick Dobson

Julius von Haast 424

Qualifications & Memberships

Research Interests

Research in our lab focuses on the structure, function and inhibition of key enzymes involved in infection and disease. We are also interested in the evolution of enzyme function, and conversely its design and manipulation.

We study a variety of enzymes: from those responsible for the biosynthesis of amino acids, in particular lysine, since these are validated drug targets; to glycolytic enzymes, such as pyruvate kinase, since these are tractable model systems to understand enzyme allostery. The list is ever increasing.

A common theme in the lab is the role protein-protein interactions in a variety of biological systems, mostly derived from bacteria, but more recently including eukaryotic proteins involved in cancer, where we hope to address the twin problems of how and why proteins form complexes and the functional consequences of these associations.

Recent Publications

  • Bencurova E., Akash A., Dobson RCJ. and Dandekar T. (2023) DNA storage—from natural biology to synthetic biology. Computational and Structural Biotechnology Journal 21: 1227-1235.
  • Davies JS., Currie MJ., North RA., Scalise M., Wright JD., Copping JM., Remus DM., Gulati A., Morado DR. and Jamieson SA. (2023) Structure and mechanism of a tripartite ATP-independent periplasmic TRAP transporter. Nature Communications 14(1)
  • King-Hudson TR., Ahuriri-Driscoll A. and Dobson R. (2023) Consulting with Māori during development of a point-of-care device; translational and experiential findings. New Zealand Scientific Review
  • McKerchar H., Dyer JM., Gerrard JA., Maes E., Clerens S. and Dobson RCJ. (2023) Characterizing lysinoalanine crosslinks in food systems: Discovery of a diagnostic ion in model peptides using MALDI mass spectrometry. Food Chemistry: X 19
  • Mckerchar HJ., Lento C., Bennie RZ., Crowther JM., Dolamore F., Dyer JM., Clerens S., Mercadante D., Wilson DJ. and Dobson RCJ. (2023) The protein dynamics of bovine and caprine β-lactoglobulin differ as a function of pH. Food Chemistry 408