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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...
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...
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 Spectrometry: Overview01:19

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...
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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Comprehensive Workflow of Mass Spectrometry-based Shotgun Proteomics of Tissue Samples
14:51

Comprehensive Workflow of Mass Spectrometry-based Shotgun Proteomics of Tissue Samples

Published on: November 13, 2021

Overcoming the dynamic range problem in mass spectrometry-based shotgun proteomics.

Linfeng Wu1, David K Han

  • 1University of Connecticut, School of Medicine, Department of Cell Biology, Farmington, Connecticut, CT 06030, USA. lwu@student.uchc.edu

Expert Review of Proteomics
|December 22, 2006
PubMed
Summary

Mass spectrometry enables large-scale protein analysis but faces challenges with complex samples. This review covers fractionation and mass spectrometry techniques for detecting low-abundance proteins in proteomics research.

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

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Area of Science:

  • Proteomics
  • Biochemistry
  • Analytical Chemistry

Background:

  • Mass spectrometry is a key technology for protein profiling and analyzing protein expression patterns in biological samples.
  • Proteomics research faces significant challenges due to the high complexity and vast dynamic range of proteins in biological mixtures.
  • Detecting low-abundance signaling proteins in complex samples is crucial for understanding cellular processes.

Purpose of the Study:

  • This review focuses on fundamental fractionation techniques used in proteomics.
  • The review covers essential mass spectrometry methods for large-scale shotgun proteomics.
  • The aim is to address the challenges of analyzing complex biological samples in proteomics.

Main Methods:

  • Exploration of various protein fractionation strategies to simplify complex mixtures.
  • Detailed examination of mass spectrometry techniques applicable to large-scale shotgun proteomics.
  • Discussion of methods for enhancing the detection of low-abundance proteins.

Main Results:

  • Fractionation is critical for managing protein complexity and dynamic range in proteomics.
  • Mass spectrometry techniques provide powerful tools for large-scale protein identification and quantification.
  • Effective methods are essential for overcoming limitations in detecting low-abundance proteins.

Conclusions:

  • Advances in fractionation and mass spectrometry are vital for the progress of proteomics.
  • Addressing the dynamic range and complexity of biological samples is paramount for comprehensive protein analysis.
  • This review provides insights into current techniques for robust shotgun proteomics.