Associate Professor Renwick Dobson
Lecturer in Biochemistry
Principle Investigator, Biomolecular Interaction Centre
Room: Biology 620
Phone: +64 3 364 2987 ext. 7646
Postal address: School of Biological Sciences, University of Canterbury, Private Bag 4800, Christchurch, New Zealand
Current Lab Members
- Rachel North (PhD)
- Katherine Donovan (PhD)
- Arvind Ravichandran (PhD)
- Jennifer Crowther (PhD)
- Chris Horne (PhD)
- Jenna Gilkes (PhD)
- Cameron MacDonald (MSc)
- Amanda Board (MSc)
Research and Publications
Renwick's UC Research Profile.
Opportunities to join the Dobson Lab
We are always looking for enthusiastic students with a sense of humor to work on projects in the Dobson Lab. If you are interested, please contact firstname.lastname@example.org. Note that international students pay the same fees as local students and you may be eligible for an international scholarship! (see http://www.canterbury.ac.nz/scholarships/)
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.
The techniques/approaches we employ in the lab include:
- X-ray crystallography
- Analytical ultracentrifugation
- Small angle X-ray and neutron scattering
- Molecular Biology (PCR, gene sub-cloning)
- Protein expression and purification
- Protein and enzyme engineering
- Multi angle laser light scattering (MALLS)
- Steady-state state kinetics
- Mass spectrometry
- Circular dichroism
- Fluorescence spectroscopy
- Isothermal titration microcalorimetry
- Protein dynamics (NMR and MD simulations, via collaborations).
Since the lab is also part of the Biomolecular Interaction Centre (http://www.bic.canterbury.ac.nz), we have access to various microscopy techniques and SPR.
The key technique of Analytical Ultra Centrifugation (AUC) is commonly used in the Lab to investigate the hydrodynamics of biomolecules, the quaternary structure of biointeractions (protein-protein, protein-DNA/RNA, protein-ligand) and can be used to determine the dissociation constants, as well and kinetic constants (koff/kon) for these interactions. We welcome collaborations employing this technique - please contact Ren (email@example.com).
Current Projects in our lab (We have PhD, Masters and Honours projects available, please email me if you are interested)
The 2 main research projects currently ongoing are summarized below:
Protein evolution –How do enzymes evolve? The process of natural selection has produced molecular catalysts with amazing performance, e.g., some enzymes can accelerate the rate of chemical transformations by factors of 106 up to 1017. Why is this process, which is based on ‘trial and error’ so rapid and efficient? We cannot easily examine the ‘fossils’ of the protein world, but we have recently gained access to the frozen ‘fossilized’ record of an evolved bacteria. In collaboration with Dr Cooper (University of Houston), this study deciphers (structurally and functionally) the evolution of E. coli pyruvate kinase as the bacterium adapts to various energy limiting environments. Because we can reproduce protein evolution in the laboratory and in real time, implementing the principles of Darwinian evolution to individual genes and enzymes, we can get a glimpse of the evolutionary intermediates, routes, and mechanisms, that may have led the way to the highly proficient enzymes known to us today. The ability to evolve proteins in the laboratory is also a powerful mean of engineering novel bespoke enzymes for a range of applications, for instance aiding synthetic organic chemistry.
Enzymology of amino acid biosynthesis – a long-standing collaboration with Prof Gerrard (University of Canterbury) & A/Prof Perugini (University of Melbourne) and more recently Dr Andre Hudson (Rochester Institute, NY).
In addition to the projects above, we collaborate with a number of different projects with Australasia:
- Dr Murphy (WEHI, Melbourne).
- Dr Michael Griffin (University of Melbourne).
- Dr Jian-guo (WEHI, Melbourne).
- Prof Jameson, Dr Williams (Massey University) & Prof Melton (University of Auckland).
- A/Prof. Cheng Hueng (University of Melbourne) and Leo Chavas (KEK, Japan).
Selected Protein Structures Solved by Dobson
Escherichia coli dihydrodipicolinate synthase (1YXC) (Strucutre in Protein Databank website)
Chalmydomonas reinhardtii diaminopimelate aminotransferase (3QGU) (Structure in Protein Databank website)
methicillin-resistant Staphylococcus aureus dihydrodipicolinate synthase (3DAQ) (Structure in Protein Databank website)