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Related Concept Videos

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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This lesson details the instrumentation of a mass spectrometer—a physical instrument to perform mass spectrometry on analyte molecules and record the characteristic mass spectra. This is achieved via three chief functions:
Mass Analyzers: Common Types01:19

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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 Spectrum: Interpretation01:24

Mass Spectrum: Interpretation

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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Mass Spectrometry: Complex Analysis

Mass spectrometry is an important technique for the identification of pure compounds. However, it has some limitations for the analysis of complex mixtures, often due to excessive fragmentation making the spectrum too complicated to decipher. Mass spectrometry can be combined with suitable separation methods in sequence, forming hyphenated methods, which are useful in the analysis of complex mixtures.
GC–MS is a powerful hyphenated method commonly used in forensics and environmental...
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Inductively Coupled Plasma–Mass Spectrometry (ICP–MS): Overview

In inductively coupled plasma–mass spectrometry (ICP–MS), an inductively coupled plasma (ICP) torch is used as an atomizer and ionizer. Solid samples are dissolved and volatilized before being introduced into the high-temperature argon plasma, while solution samples are nebulized and passed through the high-temperature argon plasma. Plasma dissociates the analytes and ionizes their component atoms to form a mixture of positive ions and molecular species. The positive ions are then passed on to...

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Measurement of Ultrafast Vibrational Coherences in Polyatomic Radical Cations with Strong-Field Adiabatic Ionization
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Implementing photodissociation in an Orbitrap mass spectrometer.

Lisa A Vasicek1, Aaron R Ledvina, Jared Shaw

  • 1Department of Chemistry and Biochemistry, The University of Texas at Austin, Austin, TX 78712, USA.

Journal of the American Society for Mass Spectrometry
|September 29, 2011
PubMed
Summary

Researchers optimized infrared multiphoton dissociation (IRMPD) in an Orbitrap mass spectrometer for enhanced peptide and protein analysis. This modification improves characterization of complex samples with high resolution and mass accuracy.

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Analysis of Volatile and Oxidation Sensitive Compounds Using a Cold Inlet System and Electron Impact Mass Spectrometry

Published on: September 5, 2014

Area of Science:

  • Analytical Chemistry
  • Mass Spectrometry
  • Biochemistry

Background:

  • Orbitrap mass spectrometers are powerful tools for high-resolution analysis.
  • Infrared multiphoton dissociation (IRMPD) is a fragmentation technique used in mass spectrometry.
  • Integrating IRMPD into existing instrument platforms can enhance analytical capabilities.

Purpose of the Study:

  • To modify a dual pressure linear ion trap Orbitrap to enable IRMPD within the higher energy collisional dissociation (HCD) cell.
  • To optimize experimental parameters for efficient IRMPD and high signal-to-noise ratio.
  • To demonstrate the utility of IRMPD-Orbitrap for characterizing various peptide and protein samples.

Main Methods:

  • Modification of a dual pressure linear ion trap Orbitrap instrument.
  • Systematic evaluation of parameters including C-trap and HCD cell pressures, C-trap radio frequency (rf) amplitude, and HCD DC offset.
  • Application of IRMPD for the analysis of phosphopeptides, supercharged peptides, N-terminal modified peptides, and top-down protein analysis.

Main Results:

  • Successful integration of IRMPD into the HCD cell of an Orbitrap mass spectrometer.
  • Optimization of key instrument parameters to enhance IRMPD efficiency and signal quality.
  • Demonstrated high-resolution and high mass accuracy analysis of modified peptides and proteins using IRMPD.

Conclusions:

  • The modified IRMPD-Orbitrap system provides a robust platform for detailed structural characterization of peptides and proteins.
  • The high resolution and mass accuracy of the Orbitrap facilitate confident identification of IRMPD-generated product ions.
  • This approach expands the capabilities of Orbitrap mass spectrometry for complex biological sample analysis.