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Postdoctoral Research Assistant - CeTPD - UOD1992

University of Dundee - School of Life Sciences

Location: Dundee
Salary: £37,174 to £45,413 per annum
Hours: Full Time
Contract Type: Fixed-Term/Contract
Placed On: 8th September 2025
Closes: 6th October 2025
Job Ref: 5669

This is an outstanding opportunity to join a recently established Research Centre that is pioneering new models of translational chemical biology and advancing the frontiers of molecular glue research. You will gain experience in world-leading, collaborative, and high-impact research at the forefront of drug discovery, with access to strong academic and industrial partnerships. We are seeking a highly motivated Postdoctoral Researcher in Structural and/or Chemical Biology to join the research group of Dr Peter Cossar at the Centre for Targeted Protein Degradation (CeTPD), University of Dundee.

The Cossar Lab integrates molecular biophysics, structural biology, and organic synthesis to develop chemical tools that address key questions in proximity-induced drug discovery, with a focus on targeting intrinsically disordered protein complexes. This Royal Society-funded position focuses on identifying molecular glues that stabilise disease-relevant protein complexes involved in Motor Neuron Disease (MND) and Frontotemporal Dementia (FTD). The position is available from the 1st of October 2025, and for a fixed-term of 3 years. The appointment will be made on University's Grade 7 salary scale (£37,174- £45,413), dependent on experience.

Your priorities will include:

  • Development of recombinant and/or cellular assays to monitor complex assembly
  • Development of Native Mass Spectrometry screening platform
  • Conduct fragment-based drug screening campaigns (non-covalent and covalent)
  • Biophysically and structurally characterize hit compound binding
  • Collaborate with team members to advance these hits into lead compounds

Who we’re looking for:

  • Familiarity with either one of the two techniques
  • Protein mass spectrometry for chemical biology and biophysics (strong preference for native MS),
  • protein–ligand structural biology (X-ray or cryo-EM) including structure-refinement tools (e.g., CCP4, PHENIX, Coot, DIALS, Cryo-Spark, Relion)
  • Experienced with biophysical assay design and troubleshooting
  • Experience with studying protein-ligand interactions and structure-based drug design
  • Cloning and DNA construct design is a plus
  • Experienced with bacterial, insect and/or human recombinant protein expression systems

For further information about this position please contact Dr Peter Cossar at p.cossar001@dundee.ac.uk. To find out more about Group/Unit/Team/School please visit https://www.dundee.ac.uk/cetpd

The Protein Degradation Centre is located in a beautiful setting overlooking the estuary of the River Tay, close to some of Scotland’s most spectacular mountain scenery. It is embedded within the University of Dundee’s School of Life Sciences, one of the premier research centres in the world recently assessed as the top UK University for Life Sciences research in the 2014 Research Excellence Framework (REF), and again in the most recent REF2021. With 900 staff from over 60 countries worldwide the School provides a dynamic, multi-national, collegiate and diverse environment with state-of-the-art laboratory, technology and teaching facilities. The University of Dundee main city- centre campus is at the heart of Dundee - an up-and-coming, friendly, compact and affordable city with a rich heritage in design and technology, that is developing into a major cultural hub. Just a short walk from the V&A Museum of Design Dundee, we’re close to both the train and bus stations.

The diversity of our staff and students helps to make the University of Dundee a UK university of choice for undergraduate, postgraduate and distance learning. Family friendly policies, staff networks for BME, Disabled and LGBT staff, membership of Athena SWAN, the ECU Race Equality Charter and Stonewall as well a full range of disability services, create an enjoyable and inclusive place to work.

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