Old Road Campus Research Building, Old Road Campus Roosevelt Drive, Headington, Oxford, OX3 7DQ
Professor Jagdeep Nanchahal
Professor Ray Owens, Professor Jim Naismith
Strubi, Rosalind Franklin Institute
Professor Chris Schofield, Dr. Akane Kawamura
Department of Chemistry
Dr Shisong Jiang
Professor John Todd, Dr Marcin Pekalski
JDRF/Wellcome Trust DIL
Dr Regent Lee, Assoc. Prof. Roman Fisher, Dr Philip Charles
Department of Surgical Sciences, Proteomics Facility, TDI
Sir Simon Lovestone, Professor Ben Davies
Department of Psychiatry & Department of Chemistry
Professor Jeremy Wells
Wageningen University & Research
Associate Professor, Biotechnology
Nicola obtained a First Class degree in Applied Biochemical Sciences from the University of Ulster, then spent a year in industry working as a molecular biologist for SmithKline Beecham. She received her D.Phil. in Molecular Microbiology at the University of Nottingham and moved back to industry to do high-throughput (HTP) cloning and validation of therapeutic cancer antigens for Oxford GlycoSciences and subsequently Celltech R&D. Nicola worked 16 years (from 2004-2020) at the SGC, University of Oxford, and since 2011 has led a team developing HTP technologies and supporting SGC projects for the production of human proteins.
My group within the Centre for Medicines Discovery (CMD) has two roles:
(1) A research group experienced in all aspects of biotechnology, molecular biology, protein biochemistry and technology development who support the CMD and other grants.
(2) A Small Research Facility (SRF) providing protein production and mass spectrometry services for internal and external academic and industrial customers.
My team generate the pipeline of clones for the CMD to determine which proteins are expressed in a soluble and stable form suitable for structural and functional studies. We have developed and optimised protocols for high-throughput ligation independent cloning, test expression and purification, large scale expression, protein production and characterisation by mass spectrometry. The platforms established by the Biotechnology team over the past 16 years whilst part of the SGC, enabled the site at Oxford to generate more than 550 novel human protein structures and 17 integral membrane protein structures. The group collaborates and interacts closely with the other CMD teams, to deliver our goals. We have established successful production systems in E. coli, insect and mammalian cells. Discovering new ways to achieve production of all types of proteins (human, viral, antigens, biomarkers, etc.) would open many doors to our long-term goals of understanding how proteins function independently, with partners and also how they interact with drugs.
Selection and structural characterization of anti-TREM2 scFvs that reduce levels of shed ectodomain.
Szykowska A. et al, (2021), Structure (London, England : 1993), 29, 1241 - 1252.e5
Identification, mapping and relative quantitation of SARS-CoV-2 Spike glycopeptides by Mass-Retention Time Fingerprinting.
Chalk R. et al, (2021), Communications biology, 4
Phospho-regulation, nucleotide binding and ion access control in potassium-chloride cotransporters.
Chi G. et al, (2021), The EMBO journal, 40
Beyond Just Peptide Antigens: The Complex World of Peptide-Based Cancer Vaccines
Stephens AJ. et al, (2021), Frontiers in Immunology, 12
Structure and activation mechanism of the human liver-type glutaminase GLS2.
Ferreira IM. et al, (2021), Biochimie, 185, 96 - 104