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Visualising protein dynamics in protein aggregation


Project Description

Proteins perform a wide variety of functions essential for life. For many proteins, the ability to undergo conformational changes while maintaining their native folded structure is essential for their function. Unfortunately, the need for protein dynamics can result in an increased risk of aggregation as ’hotspots’ that are usually buried in the core of the protein become transiently exposed, triggering an aggregation cascade.

A key question of vital importance therefore is to understand how and why proteins transiently unfold and how this causes aggregation which impacts on both on our understanding of diseases such as Parkinson’s and our ability to use proteins for biotechnology. The goal of this BBSRC Collaborative Training Partnership PhD studentship between Brockwell and Radford and our collaborators at Astra Zeneca is to use biochemical and biophysical assays to decipher how and why proteins unfold and to discover new ways of preventing aggregation.

The student employed will gain experience in molecular biology, biochemistry, protein chemistry, and cutting-edge structural and biophysical methods and will also have the opportunity to work alongside colleagues in industry.

Funding Notes

BBSRC funded Collaborative Training Partnership 4 year studentship.

Studentships covers UK/EU fees and stipend (c.£14,553) for 4 years to start in Jan 2019. Applicants should have/be expecting at least a 2.1 Hons. degree in a relevant subject. EU candidates require 3 years of UK residency in order to receive full studentship.

References

An in vivo platform for identifying inhibitors of protein aggregation
Saunders, J.C., Young, L.M., Mahood, R.A., Revill, C.H., Foster, R.J., Jackson, M.P., Smith, D.A.M., Ashcroft, A.E., Brockwell, D.J.* & Radford, S.E.* (2016) Nature Chem. Biol., 12, 94-101

Engineering the surface properties of a human monoclonal antibody prevents self-association and rapid clearance in vivo
Dobson, C.L., Devine, P.W.A., Phillips, J.J., Higazi, D.R., Lloyd, C., Popovic, B., Arnold, J., Buchanan, A., Lewis, A., Goodman, J., van der Walle, C.F., Thornton, P., Vinall, L., Lowne, D., Aagaard, A., Olsson, L.-L., Ridderstad-Wollberg, A., Welsh, F., Karamanos, T.K., Pashley, C.L., Iadanza, M.G., Ranson, N.A., Ashcroft, A.E., Kippen, A.D., Vaughan, T.J., Radford, S.E.,* & Lowe, D.C.* (2016) Sci. Reports, 6, 38644

Inducing protein aggregation by extensional flow
Dobson, J., Kumar, A., Willis, L.F., Tuma, R., Higazi, D.R., Turner, R., Lowe, D.C., Ashcroft, A.E., Radford, S.E., Kapur, N.* & Brockwell, D.J.* (2017) Proc. Nat Acad. Sci. USA, 114, 4673-4678

A new era for understanding amyloid structures and disease
Iadanza, M.G., Jackson, M.P., Hewitt, E.W., Ranson, N.A. & Radford, S.E.* (2018) Nature Rev. Mol. Cell. Biol., 19, 755–773

see also http://www.astbury.leeds.ac.uk/people/people.php and looks up Radford and Brockwell for a full list of recent publications

How good is research at University of Leeds in Biological Sciences?

FTE Category A staff submitted: 60.90

Research output data provided by the Research Excellence Framework (REF)

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