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Structural characterisation of the photosynthetic accessory protein PufX
Reference
B17913
Principal Investigator / Supervisor
Professor Michael Williamson
Co-Investigators /
Co-Supervisors
Krebs Professor of B Christopher Hunter
Institution
University of Sheffield
Department
Molecular Biology and Biotechnology
Funding type
Research
Value (£)
215,852
Status
Completed
Type
Research Grant
Start date
01/03/2003
End date
28/02/2007
Duration
48 months
Abstract
PufX is a 69-residue polypeptide that is vital for assembly and function of photosynthetic membranes from the bacterium Rb. sphaeroides. Preliminary data shows it is to be dimeric in methanol and chloroform. We shall express labelled protein in E.coli and determine the structure of this dimer using conventional NMR methods. We shall then determine the structure in detergent micelles, using conventional methods supported by paramagnetic broadening experiments. In parallel, we shall mutate key residues in PufX (eg Gly39) and identify functional and structural consequences, using spectroscopic methods and expression in Rb. sphaeroides to follow in vivo assembly. Interactions with other photosynthetic components will be analysed using crosslinking with Western blots and mass spectroscopy, and by NMR chemical shift mapping and paramagnetic broadening.
Summary
unavailable
Committee
Closed Committee - Biomolecular Sciences (BMS)
Research Topics
X – not assigned to a current Research Topic
Research Priority
X – Research Priority information not available
Research Initiative
X - not in an Initiative
Funding Scheme
X – not Funded via a specific Funding Scheme
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