Research Fellow in Structural Biology - FBSAS1085
| Dyddiad hysbysebu: | 27 Ionawr 2026 |
|---|---|
| Cyflog: | £41,064 i £48,822 bob blwyddyn |
| Oriau: | Llawn Amser |
| Dyddiad cau: | 26 Chwefror 2026 |
| Lleoliad: | Leeds, West Yorkshire |
| Gweithio o bell: | Ar y safle yn unig |
| Cwmni: | University of Leeds |
| Math o swydd: | Dros dro |
| Cyfeirnod swydd: | FBSAS1085 |
Crynodeb
Research Fellow in Structural Biology (CryoEM/ET), Astbury Centre for Structural Molecular Biology, Faculty of Biological Sciences
Salary: Grade 7 (£41,064 - £48,822 p.a.)
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 using cryoEM/ET 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 and its consequences in cells, in mouse models and in human tissue. The project will focus on IAPP involved in type-2 diabetes and -synuclein in Parkinson’s disease. For this position we are seeking a talented postdoctoral researcher with expertise in cryoEM/ET of protein assemblies. You will use cryoEM/ET to explore how changing the assembly conditions alters the structures of amyloid fibrils, and how fibril structure and polymorphism change with time in vitro, in cells and in tissues. You will also determine the structures of fibrils extracted from murine and patient samples and 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 cell biological/imaging methods.
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 Structural biology (cryoEM/ET) to elucidate protein assembly mechanisms.
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 the Government’s Skilled Worker visa page.
For research and academic posts, we will consider eligibility under the Global Talent visa. For more information, please visit visit the Government’s page, Apply for the Global Talent visa.
Salary: Grade 7 (£41,064 - £48,822 p.a.)
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 using cryoEM/ET 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 and its consequences in cells, in mouse models and in human tissue. The project will focus on IAPP involved in type-2 diabetes and -synuclein in Parkinson’s disease. For this position we are seeking a talented postdoctoral researcher with expertise in cryoEM/ET of protein assemblies. You will use cryoEM/ET to explore how changing the assembly conditions alters the structures of amyloid fibrils, and how fibril structure and polymorphism change with time in vitro, in cells and in tissues. You will also determine the structures of fibrils extracted from murine and patient samples and 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 cell biological/imaging methods.
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 Structural biology (cryoEM/ET) to elucidate protein assembly mechanisms.
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 the Government’s Skilled Worker visa page.
For research and academic posts, we will consider eligibility under the Global Talent visa. For more information, please visit visit the Government’s page, Apply for the Global Talent visa.