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

4.6K
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,...
4.6K
Protein Networks02:26

Protein Networks

2.9K
2.9K
Protein-protein Interfaces02:04

Protein-protein Interfaces

14.9K
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...
14.9K
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

4.5K
4.5K
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

14.8K
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...
14.8K
Conserved Binding Sites01:49

Conserved Binding Sites

5.2K
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...
5.2K

You might also read

Related Articles

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

Sort by
Same author

Ribonucleic acid binding protein-mediated regulation of luteinizing hormone receptor expression in granulosa cells: relationship to sterol metabolism.

Molecular endocrinology (Baltimore, Md.)·2007
Same author

Psychological stress-induced oxidative stress as a model of sub-healthy condition and the effect of TCM.

Evidence-based complementary and alternative medicine : eCAM·2007
Same author

Overexpression of OsCOIN, a putative cold inducible zinc finger protein, increased tolerance to chilling, salt and drought, and enhanced proline level in rice.

Planta·2007
Same author

Edge-based scoring and searching method for identifying condition-responsive protein-protein interaction sub-network.

Bioinformatics (Oxford, England)·2007
Same author

[The value of long-term postoperative follow-up after curative resection of lung cancer and common problems associated with it].

Nihon Geka Gakkai zasshi·2007
Same author

Identification of a type III thioesterase reveals the function of an operon crucial for Mtb virulence.

Chemistry & biology·2007

Related Experiment Video

Updated: Feb 28, 2026

Author Spotlight: Advancing Alzheimer's Research – Exploring Early Detection and Multi-Omics Approaches
09:47

Author Spotlight: Advancing Alzheimer's Research – Exploring Early Detection and Multi-Omics Approaches

Published on: December 15, 2023

2.0K

Predicting protein-protein interactions from protein sequences by a stacked sparse autoencoder deep neural network.

Yan-Bin Wang1, Zhu-Hong You, Xiao Li

  • 1Xinjiang Technical Institutes of Physics and Chemistry, Chinese Academy of Science, Urumqi 830011, China. zhuhongyou@ms.xjb.ac.cn xiaoli@ms.xjb.ac.cn.

Molecular Biosystems
|June 13, 2017
PubMed
Summary

A new computational method accurately predicts protein-protein interactions (PPIs) using protein sequence data. This approach enhances the reliability of detecting these crucial biological interactions.

More Related Videos

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

7.8K
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

2.6K

Related Experiment Videos

Last Updated: Feb 28, 2026

Author Spotlight: Advancing Alzheimer's Research – Exploring Early Detection and Multi-Omics Approaches
09:47

Author Spotlight: Advancing Alzheimer's Research – Exploring Early Detection and Multi-Omics Approaches

Published on: December 15, 2023

2.0K
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

7.8K
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

2.6K

Area of Science:

  • Computational biology
  • Proteomics
  • Bioinformatics

Background:

  • Protein-protein interactions (PPIs) are fundamental to biological processes.
  • Accurate and efficient detection of PPIs is a significant challenge.
  • High-throughput methods for PPI detection can be unreliable and incomplete.

Purpose of the Study:

  • To develop a novel computational method for predicting protein-protein interactions (PPIs) from protein sequence information.
  • To improve the accuracy and efficiency of PPI detection compared to existing methods.

Main Methods:

  • Utilized Zernike moments to extract features from Position Specific Scoring Matrices (PSSM) of protein sequences.
  • Employed stacked autoencoders for feature reconstruction.
  • Implemented a Probabilistic Classification Vector Machine (PCVM) for PPI prediction.

Main Results:

  • Achieved high average accuracies of 96.60% for Yeast and 91.19% for H. pylori PPI datasets.
  • Demonstrated superior performance compared to state-of-the-art Support Vector Machine (SVM) classifiers.
  • Successfully applied the method to predict PPIs across different species with promising outcomes.

Conclusions:

  • The proposed computational method offers a powerful, efficient, and feasible approach for predicting protein-protein interactions.
  • This work contributes significantly to advancing proteomics research by providing a more reliable PPI detection tool.