Services

Find out about the services offered in the Mass Spectrometry Facility that are offered to both internal and external customers.

Services provided include:

• Native mass spectrometry for non-covalent binding analysis (e.g. ligand-binding screens) and structural analysis
• Electrospray liquid chromatography mass spectrometry analysis
• Exact mass measurement (high resolution MS)
• Intact protein analysis
• LC-MS/MS Proteomics Mass Spec analysis and database searching

Native mass spectrometry

Native MS analyses biomolecules such as proteins and their noncovalent binding partners preserving the interactions of the partners.  This allows analysis in their folded state retaining structural information.
Native MS can be used for many protein-based applications, such as protein-protein interaction, protein-ligand binding, protein complex structures, protein folding, and antibody-drug conjugates. 
With the high-throughput sample capabilities large numbers of binding partners can be screened - for example with a view to drug discovery.

Exact mass determination

A molecular weight determination with high mass accuracy can be used to define the presence of a compound(s) in a sample. We can measure molecular weights as low as 50 Da and as high 30 kDa  with deconvolution for higher masses. 

MS/MS

MS/MS is used to determine the structure of a compound. It can be used to characterise unknown compounds, confirm identity, or sequence biopolymers.

LC/MS

LC/MS is a very effective technique to combine peak detection with peak identification. Combining chromatography with mass spectrometry allows the chromatographer to identify the chromatographic peak and to resolve co-eluting compounds of different molecular weights. Molecular weight information can confirm predicted compounds with better certainty than HPLC alone and identify  unknowns by obtaining a mass spectrum.

Proteomics

The enzymatic digest of an unknown protein can give enough information to identify it. The protein must however be from a known genome and must be fairly pure, without any other proteins present. Usually, the protein is separated from other proteins by 2-DE followed by in-gel digestion. The taxonomy of the organism and the approximate molecular weight, together with the enzymatic digest can lead to the confirmation of a particular protein being present.

Rates

Different rates apply to charity, UKRI-funded, external academic and commercial/sponsored work. Work for non-academic institutions is subject to contract. Please send an e-mail to sop.structuralchemistry@ucl.ac.uk for further enquiries

Contact Us

Telephone: 020 7753 5805/4834
Staff Email: 
andrew.weston@ucl.ac.uk 
jiajin.he@ucl.ac.uk