Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

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...
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...
Gas Chromatography–Mass Spectrometry (GC–MS)01:14

Gas Chromatography–Mass Spectrometry (GC–MS)

Gas chromatography–mass spectrometry (GC–MS) is the combination of analytical techniques of gas chromatography and mass spectrometry in a single instrument for analyzing a mixture of compounds. The gas chromatograph separates the compounds in the mixture, and the mass spectrometer analyzes each compound separately to determine the molecular masses and molecular structures.
A gas chromatograph consists of a long, narrow capillary column with a polysiloxane coating on the inner wall. The coating...
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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

High-throughput acoustic FFPE proteomics reveals ATP5IF1-associated mitochondrial alterations in acral melanoma.

Molecular & cellular proteomics : MCP·2026
Same author

From Primary Melanoma to Metastatic Evolution: AI-Powered Pathology Integrated with Functional Analysis and Clinical Metadata Improving Treatment Prediction.

Cancers·2026
Same author

Validation approach of an LC-MS/MS assay for ADA detection, applied to a Von Willebrand factor-targeted biotherapeutic.

Bioanalysis·2026
Same author

DIA-NN EasyFilter Workflow for the Fast and User-Friendly Critical Assessment and Visualization of DIA-NN Proteomics Analysis Outcome.

Journal of proteome research·2026
Same author

O-Mannose Glycosylations Influence E-Cadherin Functional Interactions.

Molecular & cellular proteomics : MCP·2026
Same author

Untargeted Plasma Proteomic Signatures and Late Graft Failure in Kidney Transplant Recipients.

Transplantation·2026

Related Experiment Video

Updated: Jun 12, 2026

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

Multidimensional chromatography coupled to mass spectrometry in analysing complex proteomics samples.

Péter Horvatovich1, Berend Hoekman, Natalia Govorukhina

  • 1Analytical Biochemistry, Department of Pharmacy, University of Groningen, Groningen, The Netherlands. p.l.horvatovich@rug.nl

Journal of Separation Science
|May 21, 2010
PubMed
Summary

Multidimensional chromatography coupled to mass spectrometry (LC(n)-MS) offers superior proteomics analysis by enhancing separation power and dynamic range. This review details LC(n)-MS methods for complex samples and differential protein expression profiling.

More Related Videos

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling
09:35

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling

Published on: April 1, 2017

Related Experiment Videos

Last Updated: Jun 12, 2026

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

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling
09:35

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling

Published on: April 1, 2017

Area of Science:

  • Analytical Chemistry
  • Proteomics
  • Biochemistry

Background:

  • Complex proteomics samples present analytical challenges for traditional 1D-LC-MS.
  • Multidimensional chromatography coupled to mass spectrometry (LC(n)-MS) significantly improves separation power and dynamic range.
  • Optimizing peak capacity and orthogonality are crucial for effective LC(n)-MS analysis.

Purpose of the Study:

  • To review key aspects of LC(n)-MS for proteomics analysis.
  • To evaluate methods for optimizing peak capacity and orthogonality.
  • To discuss data processing strategies for differential protein expression profiling using LC(n)-MS.

Main Methods:

  • Review of multidimensional chromatography techniques (e.g., RP-RP, HILIC-RP).
  • Discussion of LC(n)-MS system optimization for proteomics.
  • Analysis of data processing methods for comprehensive protein profiling.

Main Results:

  • LC(n)-MS provides greater separation power and extended dynamic range compared to 1D-LC-MS.
  • Various LC(n)-MS strategies, including RP-RP and HILIC-RP, are effective for complex shotgun proteomics.
  • Specific examples highlight the possibilities and limitations of current LC(n)-MS approaches.

Conclusions:

  • LC(n)-MS is a powerful tool for in-depth proteomics analysis.
  • Further developments in LC(n)-MS methods and data processing are needed for comprehensive differential protein expression profiling.
  • Optimized LC(n)-MS workflows enhance the analysis of complex biological samples.