The Mass Spectrometry Unit of the Collaborative Protein Technology Resource uses mass spectrometry for the study of proteins. We perform collaborative experiments with CCR researchers in areas such as: interactomes, quantitative global proteome analyses, and identification of sites of post-translational modification. In addition, we perform structural proteomics analyses. Finally, we also have an ICP-MS for analysis of inorganic atoms.
Established Technologies
Mass Spectrometry
- Characterization of protein or RNA interactomes
- Identification of proteins in complexes, organelles, subcellular fractions
- Global protein quantitation (label-free, SILAC, TMT, reductive dimethylation)
- Characterization of sites of post-translational modification, including phosphorylation, acetylation, methylation, glycosylation and ubiquitination
- Targeted quantitation of proteins
- Cross-linking mass spectrometry
- Limited proteolysis mass spectrometry
- ICP-MS analysis of inorganic atoms and compounds
- Determination of accurate mass of intact proteins
Developing Technologies
Mass Spectrometry
- Quantitation of RNA nucleosides
- Hydrogen-deuterium exchange mass spectrometry for studying protein flexibility and dynamics of conformational change in different conditions or upon interaction with a ligand