Contact Information

Primary Contact

Lisa Jenkins
Senior Associate Scientist


9000 Rockville Pike
Bethesda, MD 20892


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, 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

Major Instrumentation

  • Thermo Exploris480 Orbitrap mass spectrometer with Dionex UltiMate 3000 nanoUPLC
  • Thermo Orbitrap Fusion Lumos mass spectrometer with Dionex UlitMate 3000 nanoUPLC
  • SCIEX X500B Q-TOF mass spectrometer with Exion UPLC
  • Thermo Q Exactive Plus mass spectrometer with Dionex UltiMate 3000 UPLC
  • Thermo iCAP-Q ICP-MS mass spectrometer

User Guidelines

Projects must be approved by resource advisory committee through an online proposal process.