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

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...
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

Characterizing Antibody-Drug Conjugates with High Molecular Heterogeneity by Native Direct Mass Technology.

Analytical chemistry·2026
Same author

From Congestion to Clarity: On the Complementarity of Resolving Power and Spectral Simplification for Intact Protein Characterization.

Journal of the American Society for Mass Spectrometry·2026
Same author

Automating Middle-Down Mass Spectrometry Analysis for Extensive Antibody Characterization.

Analytical chemistry·2026
Same author

Probing Proteoform Heterogeneity From Single Human Oocytes.

Molecular & cellular proteomics : MCP·2026
Same author

Direct Readout of Multivalent Chromatin Reader-Nucleosome Interactions by Nucleosome Mass Spectrometry.

ACS central science·2026
Same author

Targeting Conformational Flexibility of a Reactive Intermediate to Enhance Selectivity of a GABA Aminotransferase Inactivator.

Journal of the American Chemical Society·2026
Same journal

Complex Indel Detection: A Simulation-Based Framework and Parsing with FreeBayes.

bioRxiv : the preprint server for biology·2026
Same journal

Emulating the gingival-tooth interface during bacterial, fungal, and viral infection in a microphysiological model of the human oral cavity.

bioRxiv : the preprint server for biology·2026
Same journal

Local SNP-explained methylation variation reveals genetically anchored and exposure-associated methylation architecture in the human brain.

bioRxiv : the preprint server for biology·2026
Same journal

Perinatal Semaglutide Treatment Improves Maternal Health and Mitigates Offspring Metabolic Dysfunction in a Mouse Model of Maternal Obesity.

bioRxiv : the preprint server for biology·2026
Same journal

Pervasive cryptic selection in the human noncoding genome.

bioRxiv : the preprint server for biology·2026
Same journal

Secreted ORF8 reprograms macrophages to enhance SARS-CoV-2 infection of lung epithelial cells.

bioRxiv : the preprint server for biology·2026
See all related articles
  1. Home
  3. Deep Proteoform Sequencing With Top-down Direct Mass Technology.
  1. Home
  3. Deep Proteoform Sequencing With Top-down Direct Mass Technology.

Related Experiment Video

Large-scale Top-down Proteomics Using Capillary Zone Electrophoresis Tandem Mass Spectrometry
10:05

Large-scale Top-down Proteomics Using Capillary Zone Electrophoresis Tandem Mass Spectrometry

Published on: October 24, 2018

Deep Proteoform Sequencing with Top-Down Direct Mass Technology.

Kenneth R Durbin, Taojunfeng Su, Ryan T Fellers

    Biorxiv : the Preprint Server for Biology
    |June 12, 2026

    View abstract on PubMed

    Summary
    This summary is machine-generated.

    Individual Ion Mass Spectrometry (I²MS) with Direct Mass Technology mode (DMTm) enhances protein analysis by improving sensitivity and resolution. This new workflow enables deep proteoform sequencing, significantly increasing sequence coverage for large proteins.

    More Related Videos

    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

    Related Experiment Videos

    Large-scale Top-down Proteomics Using Capillary Zone Electrophoresis Tandem Mass Spectrometry
    10:05

    Large-scale Top-down Proteomics Using Capillary Zone Electrophoresis Tandem Mass Spectrometry

    Published on: October 24, 2018

    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

    Area of Science:

    • Proteomics
    • Mass Spectrometry
    • Biochemistry

    Background:

    • Conventional top-down mass spectrometry faces limitations in resolving overlapping isotopic distributions, hindering deep proteoform sequencing.
    • Orbitrap mass spectrometers offer advanced capabilities for protein analysis, but further improvements in sensitivity, resolution, and mass range are desirable.

    Purpose of the Study:

    • To present an end-to-end workflow for deep proteoform sequencing using top-down mass spectrometry with Individual Ion Mass Spectrometry (I²MS) and Direct Mass Technology mode (DMTm).
    • To demonstrate the enhanced performance of DMTm compared to conventional top-down mass spectrometry methods across various fragmentation modes.
    • To introduce Proteoform Studio, a software platform for optimized ion processing and data integration to achieve comprehensive sequence coverage.

    Main Methods:

    • Utilized Individual Ion Mass Spectrometry (I²MS) with Direct Mass Technology mode (DMTm) on an Orbitrap mass spectrometer.
    • Assigned charge of individual fragment ions and converted spectra from m/z to the mass domain to resolve isotopic distributions.
    • Employed multiple fragmentation modes and integrated data from DMTm and conventional top-down methods using Proteoform Studio.

    Main Results:

    • Top-down DMTm significantly outperformed conventional methods, increasing sequence coverage for a glycosylated antibody heavy chain from 27.5% to 83.3% in 10 minutes.
    • Achieved near-complete coverage (>95%) of the internal region of a large protein, a region previously difficult to characterize.
    • Combined DMTm and conventional top-down data yielded 90.2% heavy chain sequence coverage, demonstrating complementary fragmentation patterns.

    Conclusions:

    • The developed top-down DMTm workflow enables substantially deeper proteoform sequencing with improved sensitivity, resolution, and mass range.
    • Proteoform Studio facilitates comprehensive sequence coverage by optimizing ion processing and integrating data from complementary methods.
    • This straightforward and complete workflow confidently defines proteoforms in biological systems and aids biotherapeutic development.