Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

High-Resolution Mass Spectrometry (HRMS)

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...

You might also read

Related Articles

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

Sort by

Same author

SpatioTemporal Omics Consortium: a global effort for biological discovery across species, space and time.

Nature methods·2026

Same author

Transcriptional repression by TGIF2 coordinates neurogenic priming and neural stem cell maintenance.

Science advances·2026

Same author

Comparative genomic analysis of clinically relevant human skin-associated fungi.

Nature communications·2026

Same author

Proteomics reveals spatial and molecular heterogeneities in advanced atherosclerotic carotid artery plaques.

Nature cardiovascular research·2026

Same author

The Rise of Trapped Ion Mobility Spectrometry: Principles, Applications, and Recent Developments.

Mass spectrometry reviews·2026

Same author

Aging disrupts spatiotemporal coordination in the cycling murine ovary.

Nature aging·2026

Search research articles

Related Experiment Video

Updated: Oct 2, 2025

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

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

Published on: November 15, 2017

Ultra-high sensitivity mass spectrometry quantifies single-cell proteome changes upon perturbation.

Andreas-David Brunner¹, Marvin Thielert¹, Catherine Vasilopoulou¹

¹Proteomics and Signal Transduction, Max-Planck Institute of Biochemistry, Martinsried, Germany.

Molecular Systems Biology

|February 28, 2022

Summary

We developed a mass spectrometry (MS) workflow to quantify proteins in single cells, improving sensitivity tenfold. This enables detailed analysis of cellular heterogeneity and protein changes in health and disease.

Keywords:

drug perturbation low-flow LC-MS proteomics at single-cell resolution single-cell heterogeneity systems biology

More Related Videos

Proteome-wide Quantification of Labeling Homogeneity at the Single Molecule Level

Proteome-wide Quantification of Labeling Homogeneity at the Single Molecule Level

Published on: April 19, 2019

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification

Published on: August 17, 2015

Related Experiment Videos

Last Updated: Oct 2, 2025

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

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

Published on: November 15, 2017

Proteome-wide Quantification of Labeling Homogeneity at the Single Molecule Level

Proteome-wide Quantification of Labeling Homogeneity at the Single Molecule Level

Published on: April 19, 2019

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification

Published on: August 17, 2015

Area of Science:

Proteomics
Cell Biology
Mass Spectrometry

Background:

Single-cell technologies are crucial for understanding biological complexity.
Current methods like imaging and sequencing have limitations.
Proteins drive cellular functions, making proteomic analysis of single cells highly valuable.

Purpose of the Study:

To develop a highly sensitive mass spectrometry (MS)-based workflow for single-cell proteomics.
To enable precise quantification of proteomes and their dynamics in individual cells.
To investigate cellular heterogeneity and identify novel regulatory mechanisms.

Main Methods:

Miniaturized sample preparation.
Very low flow-rate chromatography.
Novel trapped ion mobility mass spectrometry.

Main Results:

Achieved over 10-fold improvement in sensitivity for single-cell proteomics.
Precisely quantified proteomes and their changes in single, FACS-isolated cells.
Identified expected and potential novel cell cycle regulators and enabled cell phase prediction.
Revealed a stable-core proteome contrasting with stochastic transcriptome changes.

Conclusions:

The developed workflow offers unprecedented insights into cellular heterogeneity.
This technology advances ultra-high sensitivity analyses for various biological applications.
Enables deeper understanding of cellular processes in health and disease at the single-cell level.