University of Leeds
Research Fellow in Integrative Structural Molecular Biology/Biochemistry
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Research Fellow in Integrative Structural Molecular Biology/Biochemistry
Research Fellow in Integrative Structural Molecular Biology/Biochemistry, Faculty of Biological Sciences
Salary: Grade 7 (£41,064 - £48,822 p.a.)
Available on a fixed-term basis for a maximum of 13 months (1 July 2026 - 31 July 2027) (to complete specific time limited work)
This role will be based on the university campus. We are open to discussing flexible working arrangements.
Are you an ambitious researcher looking for your next challenge? Do you have an established background in protein structure/function analysis by integration of biochemical, biophysical and structural methods? Do you want to further your career in one of the UKs leading research intensive Universities?
Antibiotic resistance is projected to cause 10 million deaths per year by 2050, with gram-negative (diderm) pathogens comprising 9 of the 12 bacteria that pose the greatest threat to human health. The outer membrane (OM) of these pathogens acts as a first line of defence against an antibiotic assault and, therefore, finding ways to perturb OM assembly may deliver new routes to kill gram-negative bacteria, or sensitise them to existing antibiotics. We have been studying the mechanism by which outer membrane proteins (OMPs) reach the OM, how chaperones facilitate OMP delivery, and how the β-barrel assembly machinery (BAM) folds/inserts its clients into the OM (e.g. Schiffrin et al, Commun Biol, 2022; Csoma et al, 2025; Fenn et al, 2024; Calabrese et al, Nat Commun, 2020).
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In this project we aim to gain new information about a key player in OMP assembly, the periplasmic chaperone SurA. We have previously identified two hotspot regions on SurA that are critical for OMP recognition and now seek to address the following important questions:
What are the sequence determinants for OMP recognition and how is communication between binding sites achieved? [using NMR, ITC, native MS, peptide arrays] How does SurA modulate the conformational ensemble of its OMP clients and remodel them to ensure they remain folding-competent? [using smFRET, HX-MS, NMR and other methods] How do mutations in key hotspots alter the range of OMPs found in the OM [using proteomics] and are different hotspots on SurA responsible for binding and delivering different OMPs to BAM [using crosslinking-MS]?
Given that deletion of SurA results in OM defects, reduced pathogenicity, and loss of OM integrity, SurA could be a good target for the development of new antimicrobials.
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You will be responsible for the acquisition, analysis and integration of data obtained from a range of experimental (including smFRET, proteomics, NMR) and computational (e.g., AlphaFold) techniques, enabling the characterisation of complex and challenging systems involved in OMP chaperoning by SurA and delivery to BAM.
You will be based in the laboratories of Dr Antonio Calabrese, Professor Sheena Radford and Dr Anastasia Zhurvaleva, and work closely with collaborators at Leeds. You should have a PhD (or be close to completion) in Chemistry, Biochemistry, Biophysics or a related discipline. You will have an interest in analytical techniques, and whilst significant experience in structural biology and/or biophysics is essential, training in any areas that you lack experience will be provided.
To explore the post further or for any queries you may have, please contact:
Dr Antonio Calabrese, Associate Professor
Email: a.calabrese@leeds.ac.uk
Prof Sheena Radford, Astbury Professor of Biophysics
Email: s.e.radford@leeds.ac.uk
Dr Anastasia Zhurvaleva, Lecturer in Biological NMR Spectroscopy
Email: a.zhuravleva@leeds.ac.uk
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