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

Tandem Mass Spectrometry01:21

Tandem Mass Spectrometry

927
Tandem mass spectrometry is a technique that uses multiple mass analyzers in series to obtain a higher selectivity and signal-to-noise ratio for the analyte. 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 collision-induced...
927
Mass Spectrometry: Complex Analysis01:21

Mass Spectrometry: Complex Analysis

735
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...
735
Peptide Identification Using Tandem Mass Spectrometry01:33

Peptide Identification Using Tandem Mass Spectrometry

6.4K
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...
6.4K
Mass Spectrometers01:16

Mass Spectrometers

5.2K
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:
5.2K
Mass Spectrometry: Overview01:19

Mass Spectrometry: Overview

4.7K
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 electrospray 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...
4.7K
Mass Analyzers: Common Types01:19

Mass Analyzers: Common Types

579
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...
579

You might also read

Related Articles

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

Sort by
Same author

Alternate RNA decoding results in stable and abundant proteins in mammals.

Nature·2026
Same author

Principles of protein abundance regulation across single cells in a mammalian tissue.

bioRxiv : the preprint server for biology·2025
Same author

Slice-PASEF: Maximising Ion Utilisation in LC-MS Proteomics.

bioRxiv : the preprint server for biology·2025
Same author

Composition and RNA binding specificity of metazoan RNase MRP.

Nucleic acids research·2025
Same author

Ubiquitin-Proteasome System Dysregulation in Alzheimer's Disease Impacts Protein Abundance.

bioRxiv : the preprint server for biology·2025
Same author

Limiting the impact of protein leakage in single-cell proteomics.

Nature communications·2025
Same journal

Layered social competition coordinates reproductive hierarchy formation in ants.

bioRxiv : the preprint server for biology·2026
Same journal

Combination epigenetic-targeted therapy increases the immunogenicity of poorly immunogenic sarcomas.

bioRxiv : the preprint server for biology·2026
Same journal

Loss of LanC-like proteins delays post-injury regeneration of aging skeletal muscles.

bioRxiv : the preprint server for biology·2026
Same journal

Integrative Transfer Network: Deep Transfer Learning Across Populations and Prediction Targets.

bioRxiv : the preprint server for biology·2026
Same journal

Confidence-supported label-free metabolic imaging with FPhaS phase autofluorescence microscopy.

bioRxiv : the preprint server for biology·2026
Same journal

Sequence-encoded autoinhibition couples mRNA decapping activity to phase separation.

bioRxiv : the preprint server for biology·2026
See all related articles

Related Experiment Video

Updated: Jun 13, 2025

Automated Sample Multiplexing by using Combined Precursor Isotopic Labeling and Isobaric Tagging cPILOT
09:24

Automated Sample Multiplexing by using Combined Precursor Isotopic Labeling and Isobaric Tagging cPILOT

Published on: December 18, 2020

5.5K

Increasing mass spectrometry throughput using time-encoded sample multiplexing.

Jason Derks1, Kevin McDonnell1, Nathan Wamsley1

  • 1Parallel Squared Technology Institute, Watertown, MA 02472, USA.

Biorxiv : the Preprint Server for Biology
|June 12, 2025
PubMed
Summary
This summary is machine-generated.

Researchers developed timePlex, a novel method to increase sample analysis speed for liquid chromatography-mass spectrometry (LC-MS) proteomics. By staggering sample separations, timePlex combinatorially scales throughput, enabling sensitive analysis of single cells and significantly boosting proteomics efficiency.

More Related Videos

Analyzing Large Protein Complexes by Structural Mass Spectrometry
15:35

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Published on: June 19, 2010

24.1K
Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
12:11

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

6.8K

Related Experiment Videos

Last Updated: Jun 13, 2025

Automated Sample Multiplexing by using Combined Precursor Isotopic Labeling and Isobaric Tagging cPILOT
09:24

Automated Sample Multiplexing by using Combined Precursor Isotopic Labeling and Isobaric Tagging cPILOT

Published on: December 18, 2020

5.5K
Analyzing Large Protein Complexes by Structural Mass Spectrometry
15:35

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Published on: June 19, 2010

24.1K
Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
12:11

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

6.8K

Area of Science:

  • Proteomics
  • Analytical Chemistry
  • Biotechnology

Background:

  • Liquid chromatography-mass spectrometry (LC-MS) offers high sensitivity for analyte quantification but faces throughput limitations.
  • Current multiplexing strategies, like plexDIA, increase throughput linearly by multiplexing in the mass domain.
  • A need exists for methods that combinatorially scale proteomics throughput beyond linear increases.

Purpose of the Study:

  • To develop a novel time-domain multiplexing strategy, termed timePlex, to complement existing mass-domain multiplexing.
  • To achieve combinatorial scaling of sample throughput in LC-MS-based proteomics.
  • To demonstrate the effectiveness of timePlex for sensitive, high-throughput proteomic analyses.

Main Methods:

  • Developed timePlex, a method that staggers and overlaps sample separation periods in the time domain.
  • Combined timePlex with plexDIA (mass-domain multiplexing) for orthogonal, combinatorial multiplexing.
  • Demonstrated multiplexing of 9 samples using 3-timePlex and 3-plexDIA, and 27 samples using 3-timePlex and 9-plexDIA.

Main Results:

  • Achieved a throughput exceeding 500 samples per day with a 27-plex (3-timePlex and 9-plexDIA).
  • Demonstrated that timePlex supports sensitive analyses, including single-cell proteomics.
  • Showcased the multiplicative increase in throughput by combining time-domain and mass-domain multiplexing.

Conclusions:

  • timePlex is an effective label-free multiplexing methodology for LC-MS proteomics.
  • The combination of timePlex and plexDIA enables combinatorial scaling of proteomics throughput.
  • Projected future throughput increases exceeding 1,000 samples per day with this combined approach.