Research Associate in Photocatalytic Enzyme Design

The role

There is a PDRA post available in the group of Dr Aimee Boyle and Prof. Dek Woolfson FRS at the University of Bristol on a collaborative BBSRC-funded project (with the Universities of Manchester and Edinburgh) to develop de novo designed proteins for photo-catalysis.

Your role will be to design proteins with new structures from the bottom-up (de novo) to accommodate flavin-like moieties and substrates. You will be responsible for the rational and computational design of the proteins, developing flavination protocols, and producing and characterising the designs structurally using CD and fluorescence spectroscopy and X-ray protein crystallography. The photo-catalytic and enzymatic properties would be characterised in close collaboration with Prof. Nigel Scrutton’s FRS lab in Manchester.

Based on the above, you will need to forge good connections and communications with other members of the collaboration to fully realise the designs and evaluate their catalytic activities. Therefore, the appointed postdoc will need a combination of: expertise in the de novo design of proteins, experience in molecular biology, knowledge of protein biophysics and/or structural biology, and good communication skills.

This post is available until 31/1/28 in the first instance.

What will you be doing?

Specifically, you will design novel coiled-coil-based single-chain proteins assemblies using rationally seeded computational protein design (Chemical Science 13, 11330-11340, (2022);  Nature Chemical Biology 20, 991-999 (2024)). Designs will be produced by recombinant methods in E. coli, and characterised using a variety of techniques with which you must be familiar (e.g. circular dichroism and fluorescence spectroscopy, AUC, crystallography, SAXS, and SEC). You will also explore strategies for incorporating flavin into these scaffolds and the effects that flavin has on the folding and stability of the de novo proteins. Finally, the ability of these scaffolds to act as photocatalysts will be explored in collaboration with our partners at the University of Manchester using fast kinetics and mass spectrometry. 

You should apply if

The position would be suited to a talented and ambitious early career researcher with expertise in de novo protein design, protein production and characterisation, and an interest in enzymology. 

As the work will be in collaboration with researchers as both the Universities of Manchester and Edinburgh, it is essential that the successful candidate is keen and able to work as part of a multi-disciplinary team between these groups, and to travel to Manchester and Edinburgh as needed.

Additional information

Contract type: OE (Fixed funding until 31/01/2028)

Work pattern: 35 hours/week

Shift pattern: Monday - Friday 

This advert will close at 23:59 UK time on 14th October 2026

For informal queries please contact: Aimee Boyle aimee.boyle@bristol.ac.uk

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