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 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,...
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...
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...

You might also read

Related Articles

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

Sort by
Same author

Robust fault classification in rotary machines using recurrence quantification analysis features for machine learning techniques.

Chaos (Woodbury, N.Y.)·2026
Same author

Assessment of Artificial Intelligence (AI)-Powered Self-Care Recommendations for Management of Minor Ailments: A Comparative Analysis.

Pharmacotherapy·2025
Same author

2025 ICM: Surgical Procedure Time.

The Journal of arthroplasty·2025
Same author

Improving microvascular brain analysis with adversarial learning for OCT-TPM vascular domain translation.

Scientific reports·2025
Same author

Multiphase MRI radiomics model for predicting microvascular invasion in HCC: Development and clinical validation.

ILIVER..·2025
Same author

Assessment and Improvement of Avatar-Based Learning System: From Linguistic Structure Alignment to Sentiment-Driven Expressions.

Sensors (Basel, Switzerland)·2025
Same journal

Engineered HSP90-MP65 Bivalent Fusion Antigen: A Novel Vaccine Candidate Against Invasive Candidiasis.

Proteins·2026
Same journal

Physics-Based Energy Functions for Computational Protein Design.

Proteins·2026
Same journal

Impact of Stabilizing Osmolytes on the Conformational Dynamics of Human and Rat Islet Amyloid Polypeptides.

Proteins·2026
Same journal

Stabilization of Bone Morphogenetic Protein-2 at Physiological pH: Contrasting Roles of CHAPS and Arginine in Aggregation Inhibition.

Proteins·2026
Same journal

Structural Insights Into the Function of Leishmania major Adenylosuccinate Lyase.

Proteins·2026
Same journal

Generalizing the Gaussian Network Model: Spanning-Tree Thermodynamics Shows Entropy-Driven KRAS Activation.

Proteins·2026
See all related articles

Related Experiment Video

Updated: May 21, 2026

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling
09:35

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling

Published on: April 1, 2017

Detection of protein complexes using a protein ranking algorithm.

Nazar Zaki1, Jose Berengueres, Dmitry Efimov

  • 1Faculty of Information Technology, UAEU, Al Ain, UAE. nzaki@uaeu.ac.ae

Proteins
|June 12, 2012
PubMed
Summary
This summary is machine-generated.

A new protein ranking algorithm, ProRank, accurately detects protein complexes from protein-protein interaction networks. This method improves disease characterization for diagnostics and treatment by identifying essential proteins.

More Related Videos

Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry
14:58

Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry

Published on: November 12, 2012

Protein Complex Affinity Capture from Cryomilled Mammalian Cells
10:37

Protein Complex Affinity Capture from Cryomilled Mammalian Cells

Published on: December 9, 2016

Related Experiment Videos

Last Updated: May 21, 2026

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling
09:35

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling

Published on: April 1, 2017

Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry
14:58

Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry

Published on: November 12, 2012

Protein Complex Affinity Capture from Cryomilled Mammalian Cells
10:37

Protein Complex Affinity Capture from Cryomilled Mammalian Cells

Published on: December 9, 2016

Area of Science:

  • Computational biology
  • Systems biology
  • Bioinformatics

Background:

  • Protein complexes are crucial in disease mechanisms.
  • Accurate detection of protein complexes aids disease characterization, diagnosis, and treatment.
  • Predicting protein complexes from protein-protein interaction (PPI) networks is a significant computational challenge.

Purpose of the Study:

  • Introduce a novel protein ranking algorithm (ProRank) for detecting protein complexes.
  • Quantify protein importance using network structure and evolutionary relationships.
  • Identify essential proteins critical for cellular processes and complex formation.

Main Methods:

  • Developed ProRank, a protein ranking algorithm for PPI network analysis.
  • Utilized protein interaction structure and evolutionary relationships to quantify protein importance.
  • Evaluated ProRank on two PPI networks and two reference complex sets (81 and 162 complexes).

Main Results:

  • ProRank demonstrates competitive precision and recall in protein complex detection.
  • The algorithm accurately predicts more complexes compared to established methods like ClusterONE, CMC, CFinder, MCL, MCode, and Core.
  • Achieved a high level of accuracy, surpassing recent protein complex detection methods.

Conclusions:

  • ProRank is a highly accurate and effective method for detecting protein complexes from PPI networks.
  • The proposed method offers significant advantages over existing protein complex prediction tools.
  • ProRank's performance supports its utility in advancing disease mechanism understanding and therapeutic strategies.