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Optimization of a Digital Mass Filter for the Isolation of Intact Protein Complexes in Stability Zone 1,1.

Robert L SchraderThomas E WalkerSumeet ChakravortyGordon A AndersonPeter T A ReillyDavid H Russell
Published in: Analytical chemistry (2023)
Digital mass filters are advantageous for the analysis of large molecules due to the ability to perform ion isolation of high- m / z ions without the generation of very high radio frequency (RF) and DC voltages. Experimentally determined Mathieu stability diagrams of stability zone 1,1 for capacitively coupled digital waveforms show a voltage offset between the quadrupole rod pairs is introduced by the capacitors which is dependent on the voltage magnitude of the waveform and the duty cycle. This changes the ion's a value from a = 0 to a < 0. These effects are illustrated for isolation for single-charge states for various protein complexes up to 800 kDa (GroEL) for stability zone 1,1. Isolation resolving power ( m /Δ m ) of approximately 280 was achieved for an ion of m / z 12,315 ( z = 65+ for 800.5 kDa GroEL D398A), which corresponds to an m / z window of 44.
Keyphrases
  • heat shock protein
  • mass spectrometry
  • protein protein
  • amino acid
  • dendritic cells
  • binding protein
  • small molecule
  • simultaneous determination
  • ms ms