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Tandem Mass Spectrometry01:21

Tandem Mass Spectrometry

Tandem mass spectrometry is a technique that uses multiple mass analyzers in series to obtain a higher selectivity and reduce chemical noise during analyte detection. Instruments with multiple analyzers separated by an interaction cell enable secondary fragmentation and selected study of the fragment ions.Secondary fragmentations occur in the interaction cell and can be induced by various factors. Fragmentation induced by collision with inert gases, such as N2, Ar, He, etc., is called...
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Bond energy is the energy required to break a bond homolytically. These values are usually expressed in units of kcal/mol or kJ/mol and are referred to as bond dissociation energies when given for specific bonds or average bond energies when indicated for a given type of bond over many compounds. Firstly, the bond dissociation energy for a single bond is weaker than that of a double bond, which in turn is weaker than that of a triple bond. Secondly, hydrogen forms relatively strong bonds with...
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Thermochemical Studies of Ni(II) and Zn(II) Ternary Complexes Using Ion Mobility-Mass Spectrometry
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Higher-energy collision-activated dissociation without a dedicated collision cell.

Graeme C McAlister1, Douglas H Phanstiel, Justin Brumbaugh

  • 1Department of Chemistry, University of Wisconsin, Madison, WI 53706, USA.

Molecular & Cellular Proteomics : MCP
|March 12, 2011
PubMed
Summary
This summary is machine-generated.

Beam-type collisional activation dissociation (HCD) can now be performed in a mass spectrometer's ion injection pathway (iHCD). This method enhances isobaric tag quantitation and requires no additional hardware.

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Area of Science:

  • Analytical Chemistry
  • Mass Spectrometry
  • Proteomics

Background:

  • Beam-type collisional activation dissociation (HCD) offers advantages for peptide analysis and quantitation.
  • Conventional HCD requires specialized collision cells, limiting its accessibility.
  • Isobaric tag quantitation methods like TMT and iTRAQ benefit from efficient dissociation.

Purpose of the Study:

  • To demonstrate HCD in the ion injection pathway (iHCD) of a mass spectrometer.
  • To evaluate iHCD performance for peptide identification and isobaric tag quantitation.
  • To assess the feasibility of implementing iHCD on standard mass spectrometry hardware.

Main Methods:

  • Developed and tested an in-line HCD (iHCD) method within the ion injection pathway.
  • Analyzed complex peptide mixtures using iHCD and compared results to collision-activated dissociation (CAD).
  • Evaluated iHCD performance for isobaric tag reporter ion intensity compared to pulsed-q dissociation.

Main Results:

  • iHCD achieved comparable peptide identification rates to CAD (2883 vs. 2730 IDs).
  • Precursor-product ion conversion efficiency in iHCD was similar to dedicated collision cells.
  • iHCD produced 10-fold more intense isobaric tag reporter ions than pulsed-q dissociation.

Conclusions:

  • iHCD is a viable alternative to conventional HCD, requiring no additional hardware.
  • This method enhances isobaric tag quantitation sensitivity and can be implemented on most mass spectrometers.
  • iHCD offers a cost-effective and accessible approach for advanced peptide analysis.