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Related Concept Videos

Mass Analyzers: Common Types01:19

Mass Analyzers: Common Types

The quadrupole mass analyzer consists of four cylindrical metal rods arranged in a diamond carrying a DC voltage and a radio-frequency AC voltage. The motion of ions through the quadrupole depends on the field strength, causing only ions of a certain m/z to resonate successfully and strike the detector at a given field strength. Though the transmission rate for these analyzers is high, the exact elemental composition of the sample is not determined because of low resolution; however, they are...
Mass Analyzers: Overview01:13

Mass Analyzers: Overview

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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Ion-Exchange Chromatography

Ion-exchange chromatography, or IEC, is a technique for separating ions based on their affinity for the stationary phase. The stationary phase is a cross-linked polymer resin with covalently attached ionic functional groups. The functional groups can be either positively charged (cation exchangers) or negatively charged (anion exchangers). A cation exchanger consists of a polymeric anion and active cations, while an anion exchanger is a polymeric cation with active anions. The choice of...
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Capillary electrophoretic separations offer various modes, each with unique applications. These modes include capillary zone electrophoresis, capillary gel electrophoresis, capillary array electrophoresis, capillary isoelectric focusing, capillary isotachophoresis, micellar electrokinetic chromatography, and capillary electrochromatography.
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High-Resolution Mass Spectrometry (HRMS)01:15

High-Resolution Mass Spectrometry (HRMS)

The resolution of a mass spectrometer depends on the efficiency of separating ions with different ion masses. The mass of an atom is approximated to the sum of the masses of protons and neutrons inside, considering the masses of protons and neutrons as equal. However, the masses of the proton (1.6726 × 10−24 g) and neutron (1.6749 × 10−24 g) are not truly equal. There is a minor error in the expression of atomic masses relative to the simplest atom of hydrogen. For example, the mass of helium...
Electrospray Ionization (ESI) Mass Spectrometry01:12

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Higher molecular weight biomolecules are nonvolatile compounds that may decompose before ionizing or vaporizing during mass analysis with conventional electron impact ionization methods. Accordingly, electrospray ionization (ESI) is the favored method for vaporizing and ionizing biomolecules as it circumvents rapid fragmentation and enables the recording of mass signals for the entire biomolecule.
ESI utilizes electrical energy to transfer ions from the liquid phase of the sample into the...

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Using a Cyclic Ion Mobility Spectrometer for Tandem Ion Mobility Experiments
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High-resolution differential ion mobility separations using planar analyzers at elevated dispersion fields.

Alexandre A Shvartsburg1, David C Prior, Keqi Tang

  • 1Environmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, P.O. Box 999, Richland, Washington 99352, USA.

Analytical Chemistry
|July 30, 2010
PubMed
Summary
This summary is machine-generated.

Field Asymmetric Waveform Ion Mobility Spectrometry (FAIMS) now achieves over 200 resolving power for peptides using a stronger electric field and less Helium. This advance enhances proteomic applications by separating complex isomers.

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Area of Science:

  • Analytical Chemistry
  • Biochemistry
  • Spectrometry

Background:

  • Field Asymmetric Waveform Ion Mobility Spectrometry (FAIMS) offers orthogonality to Mass Spectrometry (MS).
  • Previous FAIMS/MS platforms had limited resolving power (∼10-20), restricting applications.
  • Recent advancements using high Helium (He) content achieved resolving power >100, enabling isomer separation.

Purpose of the Study:

  • To improve FAIMS resolving power while mitigating issues associated with high Helium concentrations.
  • To explore the impact of increased electric field strength on ion mobility separation.

Main Methods:

  • Implemented a higher separation electric field (∼35% increase over 21 kV/cm) in FAIMS.
  • Reduced Helium content to 50% in the gas mixture.
  • Analyzed multiply charged peptides to assess resolving power and ion behavior.

Main Results:

  • Achieved resolving powers >200 for multiply charged peptides, surpassing previous capabilities.
  • Demonstrated comparable or improved resolution with significantly reduced Helium percentage.
  • Observed increased ion heating and induced isomerization of labile species at higher electric fields.

Conclusions:

  • Increased electric field strength in FAIMS offers a viable alternative to high Helium concentrations for enhanced resolution.
  • This method avoids elevated pressure and Helium interference in coupled mass spectrometers.
  • The findings open new avenues for advanced proteomic and biological analyses by enabling isomer separation.