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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 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...
Conserved Binding Sites01:49

Conserved Binding Sites

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 analyses the...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.

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Related Experiment Video

Updated: Jun 23, 2026

In Vivo Functional Study of Disease-associated Rare Human Variants Using Drosophila
06:41

In Vivo Functional Study of Disease-associated Rare Human Variants Using Drosophila

Published on: August 20, 2019

Connecting protein interaction data, mutations, and disease using bioinformatics.

Jake Y Chen1, Eunseog Youn, Sean D Mooney

  • 1Informatics and Technology Complex (IT), Indiana University School of Informatics, IUPUI, Indianapolis, IN, USA.

Methods in Molecular Biology (Clifton, N.J.)
|April 22, 2009
PubMed
Summary
This summary is machine-generated.

This study integrates protein interaction and mutation data to identify disease-specific proteins. A statistical model accurately distinguishes disease-linked mutations from common variants, aiding in understanding disease mechanisms.

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Mapping Dysfunctional Protein-Protein Interactions in Disease
09:39

Mapping Dysfunctional Protein-Protein Interactions in Disease

Published on: October 24, 2025

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Last Updated: Jun 23, 2026

In Vivo Functional Study of Disease-associated Rare Human Variants Using Drosophila
06:41

In Vivo Functional Study of Disease-associated Rare Human Variants Using Drosophila

Published on: August 20, 2019

Mapping Dysfunctional Protein-Protein Interactions in Disease
09:39

Mapping Dysfunctional Protein-Protein Interactions in Disease

Published on: October 24, 2025

Area of Science:

  • Genomics
  • Proteomics
  • Computational Biology

Background:

  • Understanding genotype-phenotype correlations requires analyzing how mutations affect protein function and interactions.
  • Identifying disease-specific mutations is crucial for understanding molecular pathology.

Purpose of the Study:

  • To develop a method for integrating protein interaction and mutation data.
  • To identify disease-associated proteins and build a predictive model for mutations.

Main Methods:

  • Integration of protein-protein interaction networks with mutation datasets.
  • Development of a statistical model to analyze disease-associated mutations.
  • Application to Alzheimer's disease (AD) as a case study.

Main Results:

  • Successfully identified a subset of proteins implicated in Alzheimer's disease.
  • Achieved 83% accuracy in discriminating disease-associated mutations from single nucleotide polymorphisms (SNPs) in these proteins.
  • Visualized the statistical model of disease mutations.

Conclusions:

  • The developed method effectively integrates diverse biological data for disease-gene discovery.
  • The approach aids in pinpointing causative variants and understanding disease mechanisms.
  • This model is valuable for future research in identifying disease-causing mutations.