Research Fellow in Structural Biology

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

Required:  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.