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

8.8K
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...
8.8K
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

15.7K
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
15.7K

You might also read

Related Articles

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

Sort by
Same author

The Optimal Dose of Butorphanol Combined with Ropivacaine for Supraclavicular Brachial Plexus Block in Patients Undergoing Upper Limb Fracture Surgery: A Randomized, Double-Blind, Controlled Clinical Trial.

Drug design, development and therapy·2026
Same author

Integrated Protein Precipitation-Solid-Phase Extraction Workflow for Deep Top-Down Proteomic Analysis of Human Serum.

Journal of proteome research·2026
Same author

H<sub>2</sub>O<sub>2</sub>-free proximity proteomics for exploring dynamic protein complexes in living systems.

Nature chemical biology·2026
Same author

Developing an enzyme-assembled phytoglycogen-based carrier for intestinal-targeted delivery of metformin.

International journal of biological macromolecules·2026
Same author

Inorganic Antibody-Mimetic H-Zeolite Blocks Airborne Viruses via E340-Targeted Biorecognition.

Journal of the American Chemical Society·2026
Same author

[Native mass spectrometry and ultraviolet photodissociation reveal conformation-selectivity of zinc ion to α-synuclein].

Se pu = Chinese journal of chromatography·2026

Related Experiment Video

Updated: Apr 12, 2026

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

9.0K

[Identifying phosphopeptide by searching a site annotated protein database].

Kai Cheng, Fangjun Wang, Yangyang Bian

    Se Pu = Chinese Journal of Chromatography
    |May 12, 2015
    PubMed
    Summary

    This study introduces a novel database strategy for phosphoproteome analysis. It enhances phosphopeptide identification sensitivity and reliability by reducing the search space in shotgun proteomics.

    More Related Videos

    A Spin-Tip Enrichment Strategy for Simultaneous Analysis of N-Glycopeptides and Phosphopeptides from Human Pancreatic Tissues
    09:16

    A Spin-Tip Enrichment Strategy for Simultaneous Analysis of N-Glycopeptides and Phosphopeptides from Human Pancreatic Tissues

    Published on: May 4, 2022

    2.8K
    Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry
    11:54

    Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry

    Published on: March 23, 2020

    10.5K

    Related Experiment Videos

    Last Updated: Apr 12, 2026

    Oligopeptide Competition Assay for Phosphorylation Site Determination
    09:16

    Oligopeptide Competition Assay for Phosphorylation Site Determination

    Published on: May 18, 2017

    9.0K
    A Spin-Tip Enrichment Strategy for Simultaneous Analysis of N-Glycopeptides and Phosphopeptides from Human Pancreatic Tissues
    09:16

    A Spin-Tip Enrichment Strategy for Simultaneous Analysis of N-Glycopeptides and Phosphopeptides from Human Pancreatic Tissues

    Published on: May 4, 2022

    2.8K
    Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry
    11:54

    Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry

    Published on: March 23, 2020

    10.5K

    Area of Science:

    • Proteomics
    • Biochemistry
    • Molecular Biology

    Background:

    • Phosphoproteome analysis is crucial in proteomics.
    • Shotgun proteomics identifies phosphopeptides using variable modifications, but this increases search space and decreases sensitivity.
    • Current methods lack specificity as all residues of a type are searched, not just actual phosphorylation sites.

    Purpose of the Study:

    • To develop a more sensitive and reliable method for phosphopeptide identification in shotgun proteomics.
    • To reduce the search space in database searching for post-translation modifications (PTMs).

    Main Methods:

    • Extracted characteristic sequences from identified phosphorylation sites.
    • Created an annotated database with specific phosphorylation site information.
    • Implemented a strategy to limit variable modifications to previously identified serine, threonine, and tyrosine residues.
    • Evaluated the strategy using Mascot with diverse datasets.

    Main Results:

    • Significantly reduced the search space for phosphopeptide identification.
    • Achieved higher sensitivity in phosphopeptide identification.
    • Demonstrated high reliability of the new database searching strategy.

    Conclusions:

    • The developed annotated database strategy enhances phosphopeptide identification sensitivity and reliability.
    • This approach offers a more efficient and accurate method for phosphoproteome analysis in shotgun proteomics.