Recent Advances and Development in Mass Spectrometry

New mass spectrometry (MS) methods, collectively known as data independent analysis and hyper reaction monitoring, have recently emerged. The analysis of peptides generated by proteolytic digestion of proteins, known as bottom-up proteomics, serves as the basis for many of the protein research undertaken by mass spectrometry (MS) laboratories. Discovery-based or shotgun proteomics employs data-dependent acquisition (DDA). Herein, a hybrid mass spectrometer first performs a survey scan, from which the peptide ions with the intensity above a predefined threshold value, are stochastically selected, isolated and sequenced by product ion scanning. n targeted proteomics, selected environmental Monitoring (ERM), also known as multiple reaction monitoring (MRM), is used to monitor a number of selected precursor-fragment transitions of the targeted amino acids. The selection of the SRM transitions is normally calculated on the basis of the data acquired previously by product ion scanning, repository data in the public databases or based on a series of empirical rules predicting the Enzyme structure sites.

  • Advances in sample preparation and MS Interface design
  • Cs-SIMS,  MeV-SIMS , FIB-SIMS and In-situ liquid SIMS
  • TIMS and SSMS
  • MALDI-TOF, SELDI-TOF and TOF-SIMS
  • ICP-MS and IRMS
  • Accelerator Mass Spectrometry
  • Triple Quadrupole GC-MS/LC-MS, the next evolution
  • Physical and Biophysical Mass Spectrometry
  • Proteomic and mass spectrometry technologies for biomarker discovery
  • LC-MS & GC-MS: Mass spectroscopy (MS) detection techniques coupled to chromatographic separations
  • Advances in isolation, enrichment, derivatization and separation
  • Microfluidics combined with mass spectrometry
  • New developments in ionization and sampling
  • Ambient Mass Spectrometry (DESI, DICE, …etc)

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