- Email: firstname.lastname@example.org
- Thesis title: Folding and Chaperoning Outer Membrane Proteins: Structural Biology Guided Routes Towards New Antibiotics.
- Supervisors: Professor Sheena Radford, Professor David Brockwell
A deep rooted interest in the mechanism of biological actions was born during the time I was studying Biochemistry at the University of Birmingham. A Master's degree, also at Birmingham, in Molecular Biotechnology further cemented these interests, and widened them to include aspects of structural biology, with a focus on the β-Assembly Machinery (BAM) Complex, responsible for folding Outer Membrane Proteins (OMPs) in Gram-Negative Bacteria. Following my time at Birmingham, I have taken up a EOS Belgium funded PhD position at the Astbury Centre, under the supervision of Professor Sheena Radford, and Dr David Brockwell, where I will be further investigating Outer Membrane Biogenesis through the biochemistry of BAM-mediated OMP folding and chaperone interactions BAM and unfolded OMPs.
Gram-negative bacteria contain an asymmetric outer membrane that has been shown to contain a range of proteins involved in the pathogenicity of these species. These proteins are almost exclusively β-barrel proteins and BAM is responsible for the folding of many, if not most of these proteins into the outer membrane layer. Furthermore components of the BAM complex are conserved across Gram-negative bacteria, which therefore makes it an attractive target for the development of new antibiotics. Despite crystal and cryo-EM structures being now available for BAM, OMPs and the chaperones involved in outer membrane protein assembly there is still no molecular understanding how OMPs fold into the OM catalysed by BAM. My project aims to provide this new mechanistic understanding that will not only provide new, fundamental insights into how OMPs fold but may pave the way to the generation of new antibacterial agents.
- MSc Molecular Biotechnology
- BSc Biochemistry