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Related Concept Videos

Peptide Identification Using Tandem Mass Spectrometry01:33

Peptide Identification Using Tandem Mass Spectrometry

Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...
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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Mass Spectrometry: Overview

Mass spectrometry is an analytical technique used to determine the molecular mass and molecular formula of a compound. The basic principle of mass spectrometry is to generate ions from the analyte molecule and measure these ion abundances against their molecular mass. One common type of ionization, known as electron ionization or EI, bombards the analyte molecules in the gas phase with high-energy electron beams. The electron beams displace an electron from the molecule and leave behind a...
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Mass Spectrometers

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:
High-Resolution Mass Spectrometry (HRMS)01:15

High-Resolution Mass Spectrometry (HRMS)

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MALDI-TOF Mass Spectrometry01:19

MALDI-TOF Mass Spectrometry

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Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification
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Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Published on: November 15, 2017

A novel mass spectrometry cluster for high-throughput quantitative proteomics.

Magnus Palmblad1, Yuri E M van der Burgt, Ekaterina Mostovenko

  • 1Biomolecular Mass Spectrometry Unit, Department of Parasitology, Leiden University Medical Center, Leiden, The Netherlands. n.m.palmblad@lumc.nl

Journal of the American Society for Mass Spectrometry
|March 3, 2010
PubMed
Summary

A new mass spectrometry (MS) platform integrates Fourier transform ion cyclotron resonance (FTICR) with ion traps for faster, more accurate peptide identification and quantitation. This cost-effective system enhances proteome coverage and characterization of modifications.

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Navigating the Mass Spectrometry-Based Proteomic Data Using Free Computational Tools
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Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification
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Navigating the Mass Spectrometry-Based Proteomic Data Using Free Computational Tools

Published on: August 19, 2025

Area of Science:

  • Analytical Chemistry
  • Biochemistry
  • Mass Spectrometry

Background:

  • Fourier transform ion cyclotron resonance (FTICR) mass spectrometry offers high accuracy and resolution.
  • Ion trap mass spectrometry provides speed and economy for tandem MS.
  • Integrating these technologies presents a challenge for enhanced proteomic analysis.

Purpose of the Study:

  • To develop and implement a novel, cost-effective mass spectrometry platform.
  • To combine the strengths of FTICR and ion trap instruments for improved proteomic analysis.
  • To demonstrate the performance and capabilities of an FTICR-ion trap cluster.

Main Methods:

  • Integration of FTICR and multiple ion trap mass spectrometers using novel algorithms and software.
  • Application of chromatographic time compression to increase sample throughput.
  • Hybrid data analysis combining accurate mass from FTICR and tandem MS/MS spectra from ion traps.
  • Utilizing high resolving power and dynamic range of FTICR for label-free quantitation.
  • Employing parallel ion traps for simultaneous MS/MS experiments with diverse fragmentation techniques.

Main Results:

  • The developed FTICR-ion trap cluster achieves performance and sample throughput comparable to multiple hybrid instruments at a lower cost.
  • Peptide identification is enabled by accurate mass from FTICR and tandem MS/MS data from ion traps.
  • Precise label-free quantitation is achievable using the FTICR instrument.
  • Enhanced proteome coverage and characterization of post-translational modifications are facilitated by simultaneous MS/MS experiments.

Conclusions:

  • The FTICR-ion trap cluster represents a novel and cost-effective approach for advanced proteomic studies.
  • Chromatographic time compression is a key strategy for maximizing throughput.
  • This integrated platform offers significant advantages for peptide identification, quantitation, and PTM analysis.