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

Conjugated Proteins02:50

Conjugated Proteins

Simple proteins and protein complexes contain only amino acids. In contrast, many other proteins, called conjugated proteins, covalently bond with non-protein moieties.
Nucleoproteins are protein complexes that contain nucleic acids, categorized as deoxyribonucleoproteins (DNPs) or ribonucleoproteins (RNPs) respectively. The nucleosome is a typical example of a DNP where nuclear DNA is associated with histone proteins. The major antigen for the Covid-19 virus SARS-CoV is an RNP that is critical...
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Conjugated Proteins02:50

Conjugated Proteins

Simple proteins and protein complexes contain only amino acids. In contrast, many other proteins, called conjugated proteins, covalently bond with non-protein moieties.
Nucleoproteins are protein complexes that contain nucleic acids, categorized as deoxyribonucleoproteins (DNPs) or ribonucleoproteins (RNPs) respectively. The nucleosome is a typical example of a DNP where nuclear DNA is associated with histone proteins. The major antigen for the Covid-19 virus SARS-CoV is an RNP that is critical...
Protein Denaturation01:28

Protein Denaturation

The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...

You might also read

Related Articles

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

Sort by
Same author

S-nitrosylation of protein kinase A is required for its activation by GPCRs.

bioRxiv : the preprint server for biology·2026
Same author

Nitric oxide drives proteomic diversity through alternative splicing.

Molecular cell·2026
Same author

SPARC is associated with tumor nerve stroma interactions and perineural invasion in pancreatic ductal adenocarcinoma.

Scientific reports·2026
Same author

[Ulcerative Colitis-Associated Cancer Resembling a Submucosal Tumor-A Case Report].

Gan to kagaku ryoho. Cancer & chemotherapy·2026
Same author

The protein denitrosylase SCoR2 regulates lipogenesis and fat storage.

Science signaling·2025
Same author

Lambert W Function in Solving Delay Differential Equations for Modeling in Economics and Finance.

Nonlinear dynamics, psychology, and life sciences·2025

Related Experiment Video

Updated: Jul 7, 2026

Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study
12:43

Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study

Published on: July 27, 2016

Screening for nitric oxide-dependent protein-protein interactions.

Akio Matsumoto1, Karrie E Comatas, Limin Liu

  • 1Howard Hughes Medical Institute and Department of Medicine, Duke University Medical Center, Durham, NC 27710, USA.

Science (New York, N.Y.)
|August 2, 2003
PubMed
Summary

Nitric oxide (NO) regulates cellular signaling by mediating protein-protein interactions. Researchers identified NO-dependent interactions involving procaspase-3, acid sphingomyelinase, and NO synthase, suggesting nitrosylation is a key regulatory mechanism.

More Related Videos

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
10:24

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition
08:31

Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition

Published on: October 3, 2018

Related Experiment Videos

Last Updated: Jul 7, 2026

Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study
12:43

Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study

Published on: July 27, 2016

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
10:24

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition
08:31

Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition

Published on: October 3, 2018

Area of Science:

  • Cellular signaling
  • Molecular biology
  • Biochemistry

Background:

  • Nitric oxide (NO) is a molecule with diverse roles in cellular signaling.
  • Protein-protein interactions are crucial for cellular functions and signaling pathways.
  • Understanding how NO influences these interactions is key to deciphering cellular regulation.

Purpose of the Study:

  • To investigate the role of nitric oxide (NO) in regulating protein-protein interactions.
  • To identify novel NO-dependent binding partners of procaspase-3 using a modified yeast two-hybrid system.

Main Methods:

  • Modification of the yeast two-hybrid system to detect NO-dependent interactions.
  • Screening for binding partners of procaspase-3.
  • Validation of identified interactions in mammalian cells.

Main Results:

  • Multiple NO-dependent protein-protein interactions were identified.
  • Specific NO-dependent interactions between procaspase-3, acid sphingomyelinase, and NO synthase were confirmed in mammalian cells.
  • Evidence suggests nitrosylation is a mechanism for regulating protein interactions.

Conclusions:

  • Nitric oxide (NO) plays a significant role in modulating protein-protein interactions.
  • Nitrosylation emerges as a potential widespread mechanism for regulating protein complex formation.
  • Further proteomic studies under controlled redox conditions are warranted to uncover additional NO-mediated interactions.