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Related Concept Videos

MALDI-TOF Mass Spectrometry01:19

MALDI-TOF Mass Spectrometry

Mass spectrometry is a powerful characterization technique that can identify and separate a wide variety of compounds ranging from chemical to biological entities, based on their mass-to-charge ratio (m/z). The instruments that allow this detection, known as mass spectrometers, have three components: an ion source, a mass analyzer, and a detector. These spectrometers differ based on the nature of their ion source and analyzers.Matrix-assisted laser desorption ionization (MALDI) is a commonly...
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...
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...
Mass Spectrometry: Complex Analysis01:21

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...
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...

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Related Experiment Video

Updated: Jun 3, 2026

An HS-MRM Assay for the Quantification of Host-cell Proteins in Protein Biopharmaceuticals by Liquid Chromatography Ion Mobility QTOF Mass Spectrometry
11:09

An HS-MRM Assay for the Quantification of Host-cell Proteins in Protein Biopharmaceuticals by Liquid Chromatography Ion Mobility QTOF Mass Spectrometry

Published on: April 17, 2018

MRCQuant- an accurate LC-MS relative isotopic quantification algorithm on TOF instruments.

William E Haskins1, Konstantinos Petritis, Jianqiu Zhang

  • 1Pediatric Biochemistry Laboratory, University of Texas at San Antonio, 78249, USA.

BMC Bioinformatics
|March 17, 2011
PubMed
Summary
This summary is machine-generated.

MRCQuant improves peptide quantification in liquid chromatography-mass spectrometry (LC-MS) by addressing key challenges. This method enhances accuracy, especially for low-abundance peptides, advancing proteomics research.

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A Strategy for Sensitive, Large Scale Quantitative Metabolomics
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A Strategy for Sensitive, Large Scale Quantitative Metabolomics

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Last Updated: Jun 3, 2026

An HS-MRM Assay for the Quantification of Host-cell Proteins in Protein Biopharmaceuticals by Liquid Chromatography Ion Mobility QTOF Mass Spectrometry
11:09

An HS-MRM Assay for the Quantification of Host-cell Proteins in Protein Biopharmaceuticals by Liquid Chromatography Ion Mobility QTOF Mass Spectrometry

Published on: April 17, 2018

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification
10:37

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

Published on: November 15, 2017

A Strategy for Sensitive, Large Scale Quantitative Metabolomics
14:18

A Strategy for Sensitive, Large Scale Quantitative Metabolomics

Published on: May 27, 2014

Area of Science:

  • Proteomics
  • Analytical Chemistry
  • Biotechnology

Background:

  • Relative isotope abundance quantification is crucial for peptide identification and differential quantification in liquid chromatography-mass spectrometry (LC-MS).
  • Existing methods face challenges in LC peak boundary detection, thermal noise suppression, interference removal, and mass drift correction for time-of-flight (TOF) instruments.

Purpose of the Study:

  • To develop a novel method, MRCQuant, for robust relative isotope abundance quantification in LC-MS proteomics.
  • To address limitations in existing quantification algorithms, particularly for TOF instruments.

Main Methods:

  • Utilized the Maximum Ratio Combining (MRC) method to extract MS signal templates for interference detection/removal and LC peak boundary detection.
  • MRCQuant extracts MS templates directly from experimental data and automatically corrects for mass drift within each LC-MS run.
  • Compared MRCQuant's performance against a representative algorithm (msInspect) using public LC-MS datasets.

Main Results:

  • MRCQuant demonstrated significant improvements in the number of accurately quantified peptides.
  • The method showed enhanced performance in quantifying low-abundance peptides.

Conclusions:

  • MRCQuant effectively resolves critical issues in relative quantification for LC-MS-based proteomics.
  • The developed algorithm offers superior performance, particularly for the accurate quantification of low-abundance peptides.