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 Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.5K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
2.5K
Protein-protein Interfaces02:04

Protein-protein Interfaces

12.5K
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...
12.5K
Protein Networks02:26

Protein Networks

3.9K
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,...
3.9K

You might also read

Related Articles

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

Sort by
Same author

Navigation-Assisted Bilateral Troughing Technique for Lumbar Laminectomy: A Stepwise Approach to Safe, Teachable, and Efficient Decompression.

Cureus·2026
Same author

Pretransplant Blinatumomab Is Associated With Reduced Relapse and Improved Disease-Free Survival in Adults With B-Cell ALL Undergoing Allogeneic Hematopoietic Cell Transplantation.

Clinical lymphoma, myeloma & leukemia·2026
Same author

Glymphatic System Visualized With Intrathecal Gadoterate Meglumine Administered via External Ventricular Drain.

Cureus·2026
Same author

Cohesin and its regulation promote monopolar kinetochore orientation at meiosis I in Arabidopsis.

Current biology : CB·2026
Same author

Case Report: Complete remission of refractory Langerhans cell sarcoma following CLAG-M chemotherapy and allogeneic hematopoietic stem cell transplant.

Frontiers in oncology·2026
Same author

Composite lymphoma composed of follicular lymphoma and nodal T-follicular helper cell lymphoma: report of 3 cases highlighting histopathologic zonation of each neoplastic component.

American journal of clinical pathology·2026

Related Experiment Video

Updated: Jun 18, 2025

Detection of Protein Interactions in Plant using a Gateway Compatible Bimolecular Fluorescence Complementation BiFC System
08:21

Detection of Protein Interactions in Plant using a Gateway Compatible Bimolecular Fluorescence Complementation BiFC System

Published on: September 16, 2011

25.3K

Improved validation of protein interactions using bicistronic BiFC (Bi2FC).

Prakash Sivakumar1,2, Vijayaraj Vaishnavi1, Kothuri Gayatri1

  • 1CSIR-Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad, 500007 India.

Physiology and Molecular Biology of Plants : an International Journal of Functional Plant Biology
|August 5, 2024
PubMed
Summary
This summary is machine-generated.

This study introduces an improved in vivo method for identifying protein interactions using refolding-based Bimolecular Fluorescence Complementation (BiFC) with built-in expression control. The enhanced technique provides more reliable detection of both positive and negative protein interactions.

Keywords:
BiFCFluorescent proteinP2ATransient expressionTranslational reporters

More Related Videos

Bimolecular Fluorescence Complementation
08:54

Bimolecular Fluorescence Complementation

Published on: April 15, 2011

27.9K
Flow Cytometric Analysis of Bimolecular Fluorescence Complementation: A High Throughput Quantitative Method to Study Protein-protein Interaction
11:11

Flow Cytometric Analysis of Bimolecular Fluorescence Complementation: A High Throughput Quantitative Method to Study Protein-protein Interaction

Published on: August 15, 2013

18.4K

Related Experiment Videos

Last Updated: Jun 18, 2025

Detection of Protein Interactions in Plant using a Gateway Compatible Bimolecular Fluorescence Complementation BiFC System
08:21

Detection of Protein Interactions in Plant using a Gateway Compatible Bimolecular Fluorescence Complementation BiFC System

Published on: September 16, 2011

25.3K
Bimolecular Fluorescence Complementation
08:54

Bimolecular Fluorescence Complementation

Published on: April 15, 2011

27.9K
Flow Cytometric Analysis of Bimolecular Fluorescence Complementation: A High Throughput Quantitative Method to Study Protein-protein Interaction
11:11

Flow Cytometric Analysis of Bimolecular Fluorescence Complementation: A High Throughput Quantitative Method to Study Protein-protein Interaction

Published on: August 15, 2013

18.4K

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Cell Biology

Background:

  • Bimolecular Fluorescence Complementation (BiFC) is a key in vivo technique for detecting protein-protein interactions.
  • Existing BiFC methods often lack robust control for protein expression levels, potentially leading to inaccurate interaction results.
  • Previous studies using yeast two-hybrid (Y2H) identified certain protein pairs as non-interacting.

Purpose of the Study:

  • To develop and validate an improved BiFC method with integrated expression control for more accurate in vivo protein interaction analysis.
  • To enhance the reliability of detecting both positive and negative protein interaction results.
  • To re-evaluate previously identified non-interacting protein pairs.

Main Methods:

  • Development of a novel BiFC assay incorporating bicistronic expression of the protein of interest and a fluorescent reporter, separated by a self-cleaving peptide.
  • Validation of the improved BiFC method for robust detection of protein interactions.
  • Comparative analysis with traditional yeast two-hybrid (Y2H) assays.

Main Results:

  • The enhanced BiFC method demonstrates robust identification of positive protein interactions.
  • The assay reliably distinguishes between interacting and non-interacting protein pairs, improving the detection of absent interactions.
  • A protein pair previously identified as non-interacting by Y2H was confirmed to interact in vivo using the improved BiFC technique.

Conclusions:

  • The developed bicistronic BiFC system offers a significant advancement for in vivo protein interaction studies by incorporating essential expression controls.
  • This method enhances the accuracy and reliability of BiFC assays, reducing false positives and negatives.
  • The findings challenge previous interaction data and highlight the importance of expression normalization in protein interaction studies.