ProfessorBernadette Byrne
Associate Provost (Equality, Diversity and Inclusion)
Office of the Provost - Central Faculty
Orcid identifier0000-0001-9598-9832 (opens in a new tab)
- Associate Provost (Equality, Diversity and Inclusion)Office of the Provost - Central Faculty
- 020 7594 3004 (Work)
- 504, Sir Ernst Chain Building, South Kensington Campus, United Kingdom
RESEARCH
Recent research in our group in collaboration with Prof Alexander Cameron, University of Warwick and Prof George Diallinas, University of Athens solved the structure of the dimer of UapA, an integral membrane transporter from Aspergillus nidulans. This provided detailed insights into the mechanism of action of the protein as well as shedding light on how individual transporter molecules in a dimer arrangement can affect each others function (Alguel et al, 2016, doi: 10.1038/ncomms11336). Further work focused on understanding the role that membrane lipids have in structrue and function of UapA in collaboration with Dr Argyris Politis, University of Manchester (Pyle et al, 2018, doi: 10.1016/j.chembiol.2018.03.011).
Current work is aiming to understand the precise conformational changes associated with H+ and substrate binding of UapA in collaboration with Dr Argyris Politis, University of Manchester. Additional studies are attempting to obtain detailed insights into the mechanism of action of G-protein coupled receptor heterodimers in collaboration wtih Dr Aylin Hanyaloglu, Imperial College London.
A further area of interest are the transporters, SVCT1 and SVCT2, human homologues of UapA responsible for uptake of Vitamin C.
We are also working with Molecular Dimensions to attempt to commercialise a screen we designed that is suitable for high-throughput identification of lipids that stabilise membrane proteins in solution (Cecchetti et al, 2021, doi: 10.1371/journal.pone.0254118 ).
Finally building on the extensive work characterising therapeutic antibodies (mAbs) in different buffer conditions and on column we are starting to explore the effects that flow, experienced at various points in a mAb life cycle, have on mAb behaviour (Tiernan et al, 2022; doi: 10.1039/d1an00087j and van Haaren et al, 2024, doi: 10.1021/acs.langmuir.3c03730).
Current work is aiming to understand the precise conformational changes associated with H+ and substrate binding of UapA in collaboration with Dr Argyris Politis, University of Manchester. Additional studies are attempting to obtain detailed insights into the mechanism of action of G-protein coupled receptor heterodimers in collaboration wtih Dr Aylin Hanyaloglu, Imperial College London.
A further area of interest are the transporters, SVCT1 and SVCT2, human homologues of UapA responsible for uptake of Vitamin C.
We are also working with Molecular Dimensions to attempt to commercialise a screen we designed that is suitable for high-throughput identification of lipids that stabilise membrane proteins in solution (Cecchetti et al, 2021, doi: 10.1371/journal.pone.0254118 ).
Finally building on the extensive work characterising therapeutic antibodies (mAbs) in different buffer conditions and on column we are starting to explore the effects that flow, experienced at various points in a mAb life cycle, have on mAb behaviour (Tiernan et al, 2022; doi: 10.1039/d1an00087j and van Haaren et al, 2024, doi: 10.1021/acs.langmuir.3c03730).
GRANTS
- INTERNAL SCHEMEBBSRC UKRI IAA 22-25Biotechnology and Biological Sciences Research Cou