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Protein Networks

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 Interfaces

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...

Assembly of Signaling Complexes

Assembly of Signaling Complexes

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Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...

Microtubule Associated Proteins (MAPs)

Microtubule Associated Proteins (MAPs)

Microtubule function and architecture are regulated by an array of specialized proteins called microtubule-associated proteins or MAPs. These proteins are widespread across different organisms and have conserved protein motifs, like the multi-TOG domain for tubulin binding found in the CLASP family of MAPs. Some MAPs are lineage-specific based on their conserved domains. Their functions depend upon the cytoskeletal architecture and cell type they are located within. In-plant cells, a specific...

Protein-Protein Interfaces

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Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.

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Related Experiment Video

Updated: Oct 15, 2025

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

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

Published on: April 1, 2017

Mapping, Structure and Modulation of PPI.

Elisa Martino¹, Sara Chiarugi^1,2, Francesco Margheriti¹

¹Laboratorio NEST, Scuola Normale Superiore, Pisa, Italy.

Frontiers in Chemistry

|October 25, 2021

Summary

Understanding protein-protein interactions (PPI) is crucial for disease treatment. This review covers technologies for mapping disease-related PPIs and discovering drugs that modulate these interactions for therapeutic benefit.

Keywords:

PPI in disease1 ligand interaction5 modulation strategies3 protein-protein4 target structure2

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Last Updated: Oct 15, 2025

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

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Area of Science:

Biochemistry and Molecular Biology
Structural Biology
Pharmacology

Background:

Protein-protein interactions (PPIs) are central to numerous biological processes and are implicated in various human diseases.
Modulating PPIs offers a promising therapeutic strategy for treating complex diseases.
Understanding the molecular basis of protein complex formation is essential for drug design.

Purpose of the Study:

To review advanced technologies for mapping disease-associated PPIs.
To investigate the structure-function relationships of protein complexes.
To explore strategies for discovering ligands that modulate PPIs for therapeutic intervention.

Main Methods:

Review of current literature on technologies for PPI mapping.
Analysis of structural and functional studies of protein complexes.
Survey of drug discovery approaches targeting PPIs.

Main Results:

Identification of key technologies for characterizing disease-related PPIs.
Elucidation of structural motifs and 'hot spots' driving protein complex formation.
Overview of strategies for developing small molecules and biologics to modulate PPIs.

Conclusions:

Advanced technologies enable detailed mapping and structural investigation of disease-related PPIs.
Targeting PPIs holds significant therapeutic potential for a range of human diseases.
Further research into PPI modulation is critical for developing novel treatments.