You will have experience in the analysis of protein structure, dynamics and assembly using structural mass spectrometry methods (e.g. native mass spectrometry, chemical crosslinking, covalent footprinting and/or hydrogen-deuterium exchange), and complementary biophysical methods. This project focuses on studying the conformational dynamics and early protein-protein and protein-nucleic acid interactions that underlie phase separation mechanisms. In particular, the project will focus on studying the protein TDP-43, which plays a role in in neurodegenerative diseases, including motor neurone disease and dementia, in addition to proteins that form viral replication organelles in Rotavirus-infected cells (NSP5/NSP2). Ultimately, the understanding of membraneless organelle formation afforded by these studies may lead to new treatments for neurodegenerative disease and viral infection.
You will be based in the laboratory of Dr Antonio Calabrese (Sir Henry Dale Fellow), and will work closely with collaborators at Leeds, across the UK and internationally.
- PhD (or be close to completion) in Chemistry, Biochemistry, Biophysics or a related discipline.
- Experience in the use of structural mass spectrometry or proteomics methods is essential and working with cell biological methods would be an advantage.
- Salary: £33,797 to £40,322 p.a.Due to funding limitations it is unlikely an appointment will be made above £36,914 p.a.
- Working Time: 37.5 hour per week
- Post Type: Full Time
- Contract Type: Fixed Term (3 Years)
Application deadline: 8 December 2020