National Physical Laboratory

Protein analysis and mapping using mass spectrometry

Protein analysis and mapping using mass spectrometry 

Through work focused on the understanding of the structure-function relationship of biological molecules, NPL is using mass spectrometry (MS) techniques to characterise proteins of therapeutic or clinical interest.

Molecules are ionised and resolved according to their mass-to-charge ratio (m/z), providing information on the relative abundance of each ionic species present. For large (multi-kDalton) and structurally complex biological molecules, mass spectrometry can determine protein intact mass or detect peptide fragments, to identify the amino acid sequence (primary structure). MS can also provide other structural information, such as identities and sites of post-translational modifications. When MS is combined with other biophysical analyses, a complete profile of the primary, secondary and tertiary structures of molecules can be provided, as well as information of trace amounts of impurities.

The Bruker Autoflex II MALDI-TOF/TOF Mass Spectrometer is a high sensitivity (low fmol) reflectron and linear time-of-flight mass spectrometer, which can operate in both positive and negative ion modes to £10 ppm mass accuracy.

The Qstar Elite ESI Mass Spectrometer provides sensitive protein, peptide and metabolite coverage, by direct infusion or after chromatographic separation. Nanospray MS provides greater sensitivity (less sample consumption and more efficient ion desolvation) where required.


Customer Service tel: +44 20 8943 8637

Last Updated: 18 Aug 2015
Created: 6 May 2009


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