| Location: | Leeds |
|---|---|
| Salary: | £41,064 to £48,822 per annum |
| Hours: | Full Time |
| Contract Type: | Fixed-Term/Contract |
| Placed On: | 27th January 2026 |
|---|---|
| Closes: | 8th March 2026 |
| Job Ref: | FBSAS1084 |
This role will be based on the university campus. We are also open to discussing flexible working arrangements.
Are you an ambitious researcher looking for your next challenge? Do you have an established background in mechanistic studies of protein assembly and want to help to develop new routes to combat amyloid disease? Do you want to further your career in one of the UK’s leading research-intensive Universities?
Understanding and Controlling Amyloid Polymorphism: From Test Tube to Tissue
We are looking for an outstanding research fellow to join our interdisciplinary team investigating how proteins aggregate into amyloid fibrils, and how fibrils with different structures perturb cellular function. This 6-year Wellcome Discovery award will involve three post-doctoral fellows and two PhD students, who will form an integrated team combining biochemical, biophysical, cell biological and structural methods (cryoEM and cryoET) with the goal of transforming our understanding of amyloid polymorphism in vitro, in cells, and in mouse models and human tissue. The project will focus on IAPP involved in type-2 diabetes and a-synuclein in Parkinson’s disease. For this position we are seeking a talented postdoctoral researcher with expertise in biochemistry and cell biology, to explore how small molecules, metabolites and differences in cellular conditions influence the mechanism of amyloid assembly and alter the structures of fibrils formed. Using fluorescence methods, you will develop approaches to track fibril polymorphism and how it changes with time in test tubes, in cells and in human/murine tissue. You will also investigate fibrils extracted from murine and patient samples and to determine the role of different fibril types in causing cellular dysfunction and disease. You will work closely with two other postdoctoral fellows funded on the grant who bring expertise in biophysical analysis of amyloid assembly and structural methods (cryoEM/ET).
You will be based in the laboratories of Professors Sheena Radford and Neil Ranson, and work closely with other members of our amyloid team. For this position you should have (or be close to completing) a PhD in Biochemistry, Biophysics, Cell Biology or a related discipline, and extensive experience of using biochemical, biophysical and cell biological methods to elucidate biological mechanisms involving protein assembly.
Salary Requirements of the Skilled Worker Visa Route
Please note that this post may be suitable for sponsorship under the Skilled Worker visa route but first-time applicants might need to qualify for salary concessions. For more information please visit: www.gov.uk/skilled-worker-visa.
For research and academic posts, we will consider eligibility under the Global Talent visa. For more information please visit: https://www.gov.uk/global-talent.
What we offer in return
And much more!
To explore the post further or for any queries you may have, please contact:
Professor Sheena Radford, Astbury Professor of Biophysics
Email: s.e.radford@leeds.ac.uk
Professor Neil Ranson, Professor of Structural Molecular Biology
Email: n.a.ranson@leeds.ac.uk
Type / Role:
Subject Area(s):
Location(s):