Post-doctoral Research Fellow: Structural Mechanism of Amyloid Formation
University of Leeds - School of Molecular & Cellular Biology
|Contract Type:||Contract / Temporary|
|Placed on:||30th September 2016|
|Closes:||10th November 2016|
“The molecular mechanisms of structural conversion in amyloid disease”
Applications are invited for a Wellcome Trust-funded postdoctoral research assistant to join a dynamic interdisciplinary team focusing on using a combination of biophysical and biochemical methods to investigate the mechanisms of protein aggregation into amyloid fibrils in vitro. The project will focus on the aggregation of beta-2-microglobulin into amyloid fibrils which is associated with the disorder dialysis related amyloidosis. The person appointed will be a specialist in NMR spectroscopy applied to protein systems and will use a wide range of NMR and other biophysical methods to determine the structure and dynamics of intermediates In amyloid assembly and the molecular recognition events that govern assembly into amyloid fibrils. In addition, by mapping the interfaces involved in amyloid formation, you will develop protein aptamers able to inhibit amyloid formation and test their effects in vitro.
The project is funded jointly between the laboratories of Professors Sheena Radford, and Dr Eric Hewitt within the Astbury Centre for Structural Molecular Biology at the University of Leeds. You should have (or be close to completing) a PhD in biochemistry or a related area. Experience in NMR spectroscopy and/or characterisation of proteins using biophysical methods is required.
Click here for further information about working at the University of Leeds www.leeds.ac.uk/info/20025/university_jobs
Location: Leeds - Main Campus
Faculty/Service: Faculty of Biological Sciences
Grade: Grade 7
Salary: £32,004 to £38,183 per annum
Due to funding limitations it is unlikely an appointment will be made above £32,004 p.a.
Contract Type: Fixed Term (Until 31 December 2018)
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