Research Fellow in Biochemistry/Cell Biology

• £41,064 to £48,822
• Full time
• Fixed term: 36 months

Required: an outstanding research fellow to join an 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.