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

4.4K
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,...
4.4K
Protein Networks02:26

Protein Networks

2.7K
2.7K
Protein-protein Interfaces02:04

Protein-protein Interfaces

14.4K
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...
14.4K
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

4.3K
4.3K
Conserved Binding Sites01:49

Conserved Binding Sites

5.0K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
5.0K
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

13.9K
Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
13.9K

You might also read

Related Articles

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

Sort by
Same author

Accelerated biological aging and risk of sarcopenia: evidence from 29,000 Chinese adults.

Biology of sport·2026
Same author

Life-course metabolic vulnerability and chronic kidney disease risk after early-life famine exposure in Middle-aged and older chinese adults.

The journals of gerontology. Series A, Biological sciences and medical sciences·2026
Same author

Hydrogels in Neurological Disorders: Emerging Diagnostic and Therapeutic Applications.

International journal of nanomedicine·2026
Same author

Template-based pelvic lymph node dissection during lateral decubitus-positioned total retroperitoneal laparoscopic radical nephroureterectomy: a step-by-step description of a surgical technique.

Translational andrology and urology·2026
Same author

Nano-enabled spatially selective protein degradation modulates lactate metabolism to potentiate antitumor immunity in liver cancer.

Nature nanotechnology·2026
Same author

Glymphatic system impairment in neurological disorders: potential mechanisms and therapeutic targets.

Molecular biomedicine·2026

Related Experiment Video

Updated: Dec 27, 2025

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
06:50

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

2.4K

FCTP-WSRC: Protein-Protein Interactions Prediction via Weighted Sparse Representation Based Classification.

Meng Kong1, Yusen Zhang1, Da Xu1

  • 1School of Mathematics and Statistics, Shandong University at Weihai, Weihai, China.

Frontiers in Genetics
|March 3, 2020
PubMed
Summary

This study introduces FCTP-WSRC, a computational model for predicting protein-protein interactions (PPIs). The model achieves high accuracy across multiple datasets, offering an efficient tool for biological research.

Keywords:
crossover networkpredictionprincipal component analysisprotein–protein interactionssparse representation

More Related Videos

A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

69.6K
Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

7.6K

Related Experiment Videos

Last Updated: Dec 27, 2025

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
06:50

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

2.4K
A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

69.6K
Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

7.6K

Area of Science:

  • Computational Biology
  • Bioinformatics
  • Systems Biology

Background:

  • Understanding protein-protein interactions (PPIs) is crucial for elucidating biological processes.
  • Accurate prediction of PPIs aids in drug discovery and understanding disease mechanisms.

Purpose of the Study:

  • To develop and validate a novel computational model, FCTP-WSRC, for effective prediction of protein-protein interactions.
  • To assess the performance of FCTP-WSRC on diverse biological datasets and complex PPI networks.

Main Methods:

  • Protein sequences are mapped to numeric feature vectors using combinations of F-vector, composition (C), and transition (T).
  • Principal Component Analysis (PCA) is utilized for feature extraction to identify discriminative subspaces.
  • Weighted Sparse Representation based Classification (WSRC) is employed for the final PPI prediction.

Main Results:

  • The FCTP-WSRC model demonstrated high prediction accuracies: 96.67% for H. pylori, 99.82% for Human, and 98.09% for Yeast.
  • The model performed effectively on predicting three distinct PPI networks: single-core (CD9), multiple-core (Ras-Raf-Mek-Erk-Elk-Srf pathway), and cross-connection (Wnt-related Network).

Conclusions:

  • The proposed FCTP-WSRC method is a powerful and efficient tool for predicting protein-protein interactions.
  • The model's excellent performance across various datasets and network types suggests its broad applicability in biological research.