Whitehouse, James Michael (2022) Exploration of size and sequence in transmembrane β-barrel folding. PhD thesis, University of Leeds.
Abstract
The β-barrel assembly complex (BAM), functions to fold outer membrane proteins (OMPs) into the outer membrane of diderm bacteria. High resolution structures of BAM exist in a variety of conformations, and in complex with OMP substrates that could represent folding intermediates. Despite this, the mechanism by which BAM folds its array of OMP substrates remains unresolved.
Metadata
Supervisors: | Radford, Sheena and Brockwell, David |
---|---|
Keywords: | BAM; Membrane protein folding; de novo design; |
Awarding institution: | University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > Institute for Molecular and Cellular Biology (Leeds) |
Depositing User: | Mr James Michael Whitehouse |
Date Deposited: | 23 Mar 2023 13:00 |
Last Modified: | 23 Mar 2023 13:00 |
Open Archives Initiative ID (OAI ID): | oai:etheses.whiterose.ac.uk:32399 |
Download
Final eThesis - complete (pdf)
Embargoed until: 1 April 2026
Please use the button below to request a copy.
Filename: Whitehouse_JM_FBS_PhD_2022.pdf
Export
Statistics
Please use the 'Request a copy' link(s) in the 'Downloads' section above to request this thesis. This will be sent directly to someone who may authorise access.
You can contact us about this thesis. If you need to make a general enquiry, please see the Contact us page.