Protein Mass Spectrometry
We are a uniquely experienced mass spectrometry laboratory providing a comprehensive suite of accessible, affordable and fast analytical, functional and proteomics services to over 300 scientists across every life science department within the University, to external academic institutions across the UK and abroad as well as commercial companies from the smallest biotech start up to major multinationals. Analyses available include (but is not limited to) difficult proteins including membrane proteins, glycoproteins and macromolecular complexes; proteoform primary structure; all types of PTM characterization; chemical modification including ADCs; protein-protein interactions; protein-ligand interactions including drugs, fragments & natural ligands; ligand specificity and affinity; protein conformational fold including size, shape, stable conformers and changes in conformation; functional assays including substrate conversion; protein specific activity and monodispersity; quantitative proteomics; protein crosslinking; immunoprecipitation; small molecules, peptides & nucleic acids; absolute quantitation of drug substances from serum. We have over 28 years of MS experience and access to the latest LC-MSMS equipment and software. Please discuss your experimental requirements and obtain a quotation before submitting samples.
Our users
We provide MS services to over 300 scientists across every life science department within the University, to external academic institutions across the UK and abroad as well as commercial companies from the smallest biotech start up to major multinationals.
Working with us
Please discuss your experimental requirements and obtain a quotation before submitting samples. All data is held in strict confidence. Commercial customers may sign a service agreement including a non-disclosure clause.
Contact us
rod.chalk@cmd.ox.ac.uk 01865 617753
Analyses available
- Difficult proteins including membrane proteins, glycoproteins and macromolecular complexes (10.1016/j.cell.2018.10.037)
- Proteoform primary structure: homology, identity, mutations and domain boundaries (10.3390/chromatography1040159)
- PTM characterization: unique experience in identification, quantitation and targeted PTM mapping including phosphorylation, glycosylation, biotinylation, disulphide bonds, novel PTMs, glycopeptides and released glycans. (003-021-02455-w)
- Chemical modification: including derivitization, covalent drug binding and antibody drug conjugation
- Protein-protein interactions: including complex stoichiometry and surface contacts (10.1038/s41467-023-37035-5)
- Protein-ligand interactions: including binding of drugs, fragments, natural ligands & orphans
- Binding specificity and affinity
- Protein conformational fold: including size, shape, stable conformers and changes in conformation (10.1042/BCJ20170527)
- Functional assays: including substrate conversion, transport and stability (10.1101/2020.05.13.093849)
- Protein quality control, specific activity, monodispersity, purity and contaminant identification
- Quantitative proteomics: heavy isotope labelled or label-free quantitation using DDA or DIA fragmentation.
- Protein crosslinking
- Immunoprecipitation analysis
- Small molecules, peptides & nucleic acids (10.1038/s41557-021-00866-0)
- Absolute quantitation: including MRM drug quantitation from serum (10.1172/JCI130571)
Staff
Dr Rod Chalk trained in biological mass spectrometry at QUB in 1996. He worked in instrument development and protein characterisation in Biotech and Pharma industries before joining the SGC in 2007. His research interests include the mechanism of electrospray ionisation and how to apply this to structural biology and drug discovery.
Dr Kavya Clement joined the lab in 2022, as Postdoctoral Scientist specialising in Mass Spectrometry. She gained her PhD in Nano-Biochemistry from CEA in Grenoble, France working with nano-electro-mechanical-sensor mass spectrometry (NEMS-MS). Previously, she obtained an integrated Master’s degree in Nanotechnology from Amity University, India which led to her working thereafter to develop a biosensor at CNR, Italy.
Equipment
(NDMRB site) Bruker TIMS-TOF Pro, (Biochemistry site) Agilent 6520 QTOF, Agilent 1969 TOF, Bruker Amazon ETD
Software
We operate an in-house Mascot server, and use proprietary vendor software including Masshunter, DA and Biotools as well as specialist tools developed in-house. Our proteomics data is compatible with downloadable open source software such as DIA-NN and MaxQuant, and we encourage users to use these tools.