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The mass analyzer is a crucial component of the mass spectrometer. In the ionization chamber, the vaporized sample is bombarded with a high-energy electron beam to generate a radical cation and further fragment into neutral molecules, radicals, and cations. A series of negatively charged accelerator plates accelerate the cations into the mass analyzer. The mass analyzer separates ions according to their mass-to-charge (m/z) ratios and then directs them to the detector. The common types of mass...
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An unknown compound can be established by identifying the molecular ion peak in the mass spectrum. The molecular ion peak is often weak or absent due to the predominance of fragmentation in high-energy electron beams. In such cases, a soft-energy electron beam can be used to scan the spectrum to enhance the intensity of the molecular ion peak. Additionally, chemical ionization, field ionization, and desorption ionization spectra are used to obtain a relatively intense molecular ion peak.To...
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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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Native IM-Orbitrap MS: Resolving What Was Hidden.

Michael L Poltash1, Jacob W McCabe1, Mehdi Shirzadeh1

  • 1Department of Chemistry, Texas A&M University, 3255 TAMU, College Station, Texas 77843.

Trends in Analytical Chemistry : TRAC
|March 20, 2020
PubMed
Summary
This summary is machine-generated.

Native ion mobility-mass spectrometry (IM-MS) enhances protein analysis by improving duty-cycle efficiency. This advanced technique allows for more accurate measurements of protein structure and dynamics.

Keywords:
Fourier transform-ion mobilityIon mobility-mass spectrometryOrbitrap mass spectrometerhigh resolution mass spectrometryintact protein complexesion mobilitymembrane proteinnative mass spectrometryperiodic focusing drift tube ion mobilityprotein-ligand interactions

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Area of Science:

  • Biophysical Chemistry
  • Analytical Chemistry
  • Structural Biology

Background:

  • Native ion mobility-mass spectrometry (IM-MS) is an emerging technique for studying protein structure and function.
  • Accurate determination of ion-neutral collision cross sections and high-resolution mass measurements are crucial for detailed biomolecular analysis.

Purpose of the Study:

  • To address the duty-cycle mismatch in IM-MS instruments.
  • To enhance the efficiency and applicability of IM-MS for complex biological samples.

Main Methods:

  • Utilizing a frequency modulated drift tube coupled with an Orbitrap mass spectrometer.
  • Implementing a multiplexed data acquisition strategy to overcome duty-cycle limitations.
  • Applying Fourier transform to convert frequency-domain data to ion mobility drift times.

Main Results:

  • Achieved a 25% duty-cycle, a significant improvement over traditional methods (<1%).
  • Enabled accurate analysis of intact protein complexes with enhanced mobility and mass resolution.
  • Demonstrated the potential for capturing dynamic changes in protein structures.

Conclusions:

  • The developed IM-Orbitrap MS method offers a highly efficient and sensitive approach for structural proteomics.
  • This technique advances the capability to investigate protein structure, dynamics, and interactions in their native states.
  • The improved duty-cycle and resolution open new avenues for analyzing complex biological systems.