Tiffany finishes Honours!

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Congratulations to Tiffany Chau, who has recently finished off a challenging but rewarding Honours year in the Jackson Lab! Well done Tiffany!

 

 

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

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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”

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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.

New Nature Chemical Biology paper

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Nature Chemical Biology Abstract Binding protein to enzyme Jackson Clifton

 

It’s out! Our Nature Chemical Biology paper “Evolution of cyclohexadienyl dehydratase from an ancestral solute-binding protein” is now online. 

How do new enzymes evolve from proteins that were initially specialised for binding? In this work, we use ancestral protein reconstruction to calculate and characterise the evolutionary intermediate states linking an ancestral solute-binding protein to the extant enzyme cyclohexadienyl dehydratase. We show how the intrinsic reactivity of a desolvated general acid was harnessed by a series of mutations radiating from the active site, which optimized enzyme–substrate complementarity and transition-state stabilization and minimized sampling of noncatalytic conformations.

2018 Lorne Conference on Protein Structure and Function

The group had a great time down at the Lorne Protein Conference last week. So much great science, and an absolutely beautiful location! Matt S, Vanessa, Galen and Joe presented posters on their work. Congratulations to Galen and Joe for picking up poster prizes! Top work guys.

The week was topped off with a fabulous day at the Lorne Protein Engineering Satellite Conference which was held at the Florey Institute of Neuroscience and Mental Health, Melbourne. So much exciting work happening in the field!

 

Welcome Dr Matthew Wilding!

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We are very happy to welcome Dr Matthew Wilding to our group. Matt obtained his Ph.D. from the University of Manchester (UK) in 2012 and moved to Australia to take up a postdoctoral research position at the Commonwealth Scientific and Industrial Research Organisation (CSIRO). He was subsequently appointed as a Research Scientist at CSIRO, working in the CSIRO Biocatalysis Team.  Matt has recently taken up a joint appointment between CSIRO and ANU as a Synthetic Biology Research Fellow, based at the Research School of Chemistry. Matt is (amongst many other things) currently aiming to re-engineer the translation machinery of E. coli to develop a high-throughput screen for peptide translation.

You can read more about Matt and find a list of his projects and publications here:

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