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

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

15.4K
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...
15.4K
Phosphorylation01:02

Phosphorylation

55.2K
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
55.2K
Phosphorylation01:02

Phosphorylation

7.8K
7.8K
Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

2.8K
Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
2.8K

You might also read

Related Articles

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

Sort by
Same author

Stirring glycopeptides away from the constraints of solid-phase synthesis misconceptions.

Frontiers in molecular biosciences·2026
Same author

Total Synthesis of Conjugation-Ready Sulfated Red Algae Carrageenan Oligosaccharides for Sensing Applications.

Journal of the American Chemical Society·2026
Same author

Expeditious synthesis of multiglycopeptides with heterogeneous glycan cores derived from an α-dystroglycan mucin-like domain.

Organic & biomolecular chemistry·2026
Same author

Expeditious Synthesis of Multiglycosylated Peptides for Sensing of <i>Listeria monocytogenes</i>.

Journal of medicinal chemistry·2025
Same author

Monosaccharide-Derived Enantioselectivity in SWCNT Chemoresistive VOC Sensing.

Chemistry (Weinheim an der Bergstrasse, Germany)·2025
Same author

FibrilPaint to determine the length of Tau amyloids in fluids.

Proceedings of the National Academy of Sciences of the United States of America·2025

Related Experiment Video

Updated: Mar 14, 2026

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

9.0K

Methods for studying the effects of phosphorylation patterns in proteins.

Shachar Guy Bressler1, Dana Grunhaus1, Mattan Hurevich1

  • 1The Institute of Chemistry, The Hebrew University of Jerusalem, Edmond J. Safra Campus, Givat Ram, Jerusalem 91904, Israel.

Biochemical Society Transactions
|March 13, 2026
PubMed
Summary

Understanding protein phosphorylation patterns is crucial for cell function and disease. This review details methods for studying these patterns, emphasizing complementary approaches for comprehensive analysis.

Keywords:
multiphosphorylationpeptidesphosphorylationproteins

More Related Videos

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

19.4K
Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein
11:23

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Published on: June 30, 2019

6.8K

Related Experiment Videos

Last Updated: Mar 14, 2026

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

9.0K
Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

19.4K
Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein
11:23

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Published on: June 30, 2019

6.8K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Regulation

Background:

  • Protein phosphorylation is a key cellular regulatory mechanism with diverse functional and pathological outcomes.
  • The complexity arises from multiple phosphorylation sites on proteins, creating numerous patterns.
  • Linking specific phosphorylation patterns to biological functions is a significant experimental hurdle.

Purpose of the Study:

  • To review and compare strategies for studying protein phosphorylation patterns.
  • To highlight the complementary nature of different experimental approaches.
  • To provide a practical toolbox for dissecting phosphorylation pattern regulation.

Main Methods:

  • Cellular approaches: phosphomimetics, kinase assays, genetic code expansion.
  • In vitro methods: enzymatic phosphorylation, semi-synthetic phosphoproteins.
  • Synthetic phosphopeptide libraries for precise phosphosite control at the domain level.

Main Results:

  • Cellular methods offer native environment studies but have drawbacks.
  • In vitro methods provide mechanistic insights but have low yields and scalability issues.
  • Synthetic phosphopeptide libraries enable precise mapping of phosphorylation patterns at the domain level.

Conclusions:

  • No single method is sufficient; complementary approaches are ideal.
  • Combining cellular, in vitro, and peptide library methods offers a comprehensive strategy.
  • Integrated methods are essential for dissecting how phosphorylation patterns regulate protein behavior.