High-resolution mass spectrometry for in vivo proteome dynamics using heavy water metabolic labeling

Research output: Contribution to journalArticlepeer-review

5 Scopus citations


Cellular proteins are continuously degraded and synthesized. The turnover of proteins is essential to many cellular functions. Combined with metabolic labeling using stable isotopes, LC–MS estimates proteome dynamics in high-throughput and on a large scale. Modern mass spectrometers allow a range of instrumental settings to optimize experimental output for specific research goals. One such setting which affects the results for dynamic proteome studies is the mass resolution. The resolution is vital for distinguishing target species from co-eluting contaminants with close mass-to-charge ratios. However, for estimations of proteome dynamics from metabolic labeling with stable isotopes, the spectral accuracy is highly important. Studies examining the effects of increased mass resolutions (in modern mass spectrometers) on the proteome turnover output and accuracy have been lacking. Here, we use a publicly available heavy water labeling and mass spectral data sets of murine serum proteome (acquired on Orbitrap Fusion and Agilent 6530 QToF) to analyze the effect of mass resolution of the Orbitrap mass analyzer on the proteome dynamics estimation. Increased mass resolution affected the spectral accuracy and the number acquired tandem mass spectra.

Original languageEnglish (US)
Article number7821
Pages (from-to)1-13
Number of pages13
JournalInternational journal of molecular sciences
Issue number21
StatePublished - Nov 1 2020


  • High resolution MS
  • LC–MS
  • Protein turnover
  • Rate constant

ASJC Scopus subject areas

  • Catalysis
  • Molecular Biology
  • Spectroscopy
  • Computer Science Applications
  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Inorganic Chemistry


Dive into the research topics of 'High-resolution mass spectrometry for in vivo proteome dynamics using heavy water metabolic labeling'. Together they form a unique fingerprint.

Cite this