Galen hits ‘Submit’ on his PhD Thesis!


Congratulations to Galen Correy who submitted his PhD thesis last week! Here he is clicking on the ‘submit’ button. Well done Galen!


Check out a few of Galen’s papers:






Ben Clifton awarded ‘Best Thesis’

Ex-Jackson group member Dr. Ben Clifton has been awarded the ‘ANU Research School of Chemistry Director’s award for the Best Thesis 2017’. Ben’s PhD thesis ‘Functional evolution of solute-binding proteins’ describes the use of ancestral protein reconstruction to explore the molecular evolution of binding specificity and catalysis in amino-acid binding proteins.

You can find some of Ben’s published work here:


Congratulations Ben!

New Nature Chemical Biology paper!

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Image result for Monitoring hippocampal glycine with the computationally designed optical sensor GlyFS


Link to paper

The amino acid glycine is an important inhibitory neurotransmitter and co-agonist of the N-methyl-D-aspartate receptors involved in synaptic plasticity. In this work, published in Nature Chemical Biology, we describe the computational design, development, and application of the first optical sensor for glycine. This FRET sensor can be used with single and two-photon excitation fluorescence microscopy. Here, we show that it can be used in combination with electrophysiology to investigate the spatial distribution of glycine in the extracellular space, and to probe how glycine concentrations change in response to plasticity-inducing stimuli.

This work was done in collaboration with Christian Henneberger’s group (University of Bonn, Institute of Cellular Neurosciences). Congratulations to Will, Michel and everyone involved in this work.


Modulating enzyme activity via incorporation of non-canonical amino acids – new chapter


Colin and Jules have recently published a chapter, with Thomas Huber (ANU), about using non-canonical amino acids for the modulation of enzyme activity. This chapter, published in Modern Biocatalysis: Advances Towards Synthetic Biological Systems (RSC Publishing), outlines the use of unnatural amino acids (UAAs) in protein engineering. Examples of how UAAs have successfully been used to engineer proteins for enhanced thermostability, catalytic efficiency, specificity and selectivity are provided, and remaining challenges within the field are discussed. This work also describes the engineering of tRNA synthetases for the site-specific incorporation of UAAs into proteins.

The chapter can be found here.


New Publication! – “Hydrogel-Immobilized Supercharged Proteins”



Immobilizing enzymes on a solid support can help improve their stability, rendering them more suitable for industrial and medical applications. However, standard covalent attachment approaches can be costly, often require many steps, and commonly lead to unfavourable orientations of the enzymes on the solid media. In this work, recently published in Advanced Biosystems, we produced enzyme-hydrogel complexes using anionic hydrogels and an engineered cationic supercharged phosphotriesterase. We show this system is capable of detoxifying organophosphates and catalyzing enantioselective reactions, and is remarkably robust and long-lasting (even when exposed to organic solvents). Additionally, degraded enzyme can be easily stripped from the gel and replaced with fresh protein, resulting in a very flexible system that could be readily scaled up for use in industry, synthesis, and bioremediation. Congratulations to Eleanor and everyone involved with this project.