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Related Concept Videos

Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
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...
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...
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...
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...

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Navigating the Mass Spectrometry-Based Proteomic Data Using Free Computational Tools
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Navigating the Mass Spectrometry-Based Proteomic Data Using Free Computational Tools

Published on: August 19, 2025

Mass spectrometry-driven proteomics: an introduction.

Kenny Helsens1, Lennart Martens, Joël Vandekerckhove

  • 1Department of Medical Protein Research, VIB, Ghent University, B-9000, Ghent, Belgium. kenny.helsens@vib-ugent.be

Methods in Molecular Biology (Clifton, N.J.)
|May 24, 2011
PubMed
Summary
This summary is machine-generated.

This review explores protein analysis, covering protein synthesis, folding, and function. It discusses methods for understanding protein presence, localization, modification, and context in molecular biology.

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A Streamlined Approach for Mass Spectrometry-Based Proteomics Using Selected Tissue Regions
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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
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Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Published on: November 15, 2017

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Proteins are central to biological functions.
  • Protein life cycle involves tightly regulated synthesis and folding.
  • Understanding protein roles is crucial for deciphering cellular phenotypes.

Purpose of the Study:

  • To review methods for protein analysis.
  • To discuss recent advances in large-scale protein analysis (proteomics).
  • To cover principles of protein presence, localization, modification, and context.

Main Methods:

  • Review of established and recent techniques in protein analysis.
  • Discussion of principles underlying various protein detection and characterization methods.
  • Focus on large-scale proteomics approaches.

Main Results:

  • Proteins exhibit diverse functions including complex formation, receptor activity, and signal transduction.
  • Protein analysis requires annotation of presence, localization, modification state, and biochemical context.
  • Numerous methods have been developed for comprehensive protein analysis.

Conclusions:

  • Protein analysis is a key area in molecular biology.
  • Advances in proteomics offer powerful tools for studying proteins.
  • A thorough understanding of protein dynamics is essential for biological research.