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Designer Cross-Linking Chemistry To Probe Protein-Protein Interactions in vivo

Project Description

A key problem in life-sciences research is to understand cellular processes with molecular and temporal resolution – this would allow the identification of the transient intermediates that play key roles in the function of biomacromolecular machines, signaling, translocation and folding. The goal of this project is to develop covalent cross-linking reagents that possess (1) suitably reactive groups for high-yielding cross-linking over a variety of timescales and (2) handles (fluorophores, affinity groups) for analyses in cells. We will then use these reagents to study the interactome of outer membrane proteins (OMPs) the beta-barrel assembly machinery (BAM) and relevant chaperones of Gram negative bacteria. The results will open the door to new methods for delineating molecular reactions in cells, in general, as well as to elucidate how OMPs fold- a question of critical importance and utility in the drive to develop new antimicrobial agents that target this pathway.

Funding Notes

White Rose BBSRC Doctoral Training Partnership in Mechanistic Biology
4 year fully-funded programme of integrated research and skills training, starting Oct 2019:
• Research Council Stipend
• UK/EU Tuition Fees
• Conference allowance
• Research Costs

At least a 2:1 honours degree or equivalent. We welcome students with backgrounds in biological, chemical or physical sciences, or mathematical backgrounds with an interest in biological questions.
EU candidates require 3 years of UK residency in order to receive full studentship

Not all projects advertised will be funded; the DTP will appoint a limited number of candidates via a competitive process.

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1. C.M. Grison, J. A. Miles, S. Robin, A. J. Wilson*, D. J. Aitken*: An α-Helix-Mimicking 12,13-Helix: Designed α/β/γ-Foldamers as Selective Inhibitors of Protein–Protein Interactions, Angew. Chem. Int. Ed., 2016, 55, 11096–11100.
2. G. Preston, S. E. Radford, A. J. Wilson*: Analysis of Amyloid Nanostructures Using Photo-Crosslinking: In Situ Comparison of Three Widely Used Photo-Crosslinkers, ACS Chem. Biol., 2014, 9, 761–768
3. G. Preston, S. E. Radford, A. E. Ashcroft, A. J. Wilson*: Covalent cross-linking within supramolecular peptide structures, Anal. Chem., 2012, 84, 6790–6797.
4. J.C. Saunders, L.M. Young, R.A. Mahood, C. H. Revill, R. J. Foster, M. P. Jackson, D. A. M. Smith, A. E. Ashcroft, D. J. Brockwell, S. E. Radford, An in vivo platform for identifying inhibitors of protein aggregation Nature Chem. Biol., 2016 12, 94-101
5. F. Stull, P. Koldewey, J. R. Humes, S. E. Radford, J. C. A. Bardwell, Substrate protein folds while it is bound to the ATP-independent chaperone Spy Nat. Struct. Mol. Biol. 2016, 1, 53-59

How good is research at University of Leeds in Chemistry?

FTE Category A staff submitted: 34.40

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

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