Are you looking to apply your skills to gain a new molecular understanding of the mechanism of amyloid formation and help to develop new routes to combat amyloid disease?
We are looking for an outstanding postdoctoral research fellow to join our interdisciplinary team that is investigating how proteins aggregate into amyloid fibrils, including the link between disease-relevant mutations, post-translational modifications and fibril structure. Funded by Wellcome, you will use biological NMR and other biochemical and biophysical methods, including mass spectrometry, single molecule FRET and other biophysical methods to map the early protein-protein interactions in amyloid formation and to discover new routes to prevent or control these interactions using small molecules, chaperones, or other approaches. You will have expertise in the analysis of protein structure and dynamics using modern biomolecular NMR approaches combined with computational analysis and/or other biophysical and biochemical methods to interrogate how ligands bind and affect protein assembly. The project will focus on a range of amyloid diseases, including type II diabetes, Parkinson’s and systemic amyloidosis.
You will be based in the laboratory of
Professor Sheena Radford and work closely with other members of our amyloid group that bring skills in cryoEM, biophysics, cell biology and peptide chemistry to the team (Radford lab). You should have a PhD (or be close to completing one) in Structural Biology, Chemical Biology, Biochemistry, Biophysics or a related discipline, and you should have extensive experience of using biological NMR and other biophysical methods to elucidate biological mechanisms.
To explore the post further or for any informal queries you may have, please contact:
Professor Sheena Radford, Astbury Professor of Biophysics
Tel: +44 (0)113 343 3170 | Email: