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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

15.0K
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...
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Protein-Protein Interfaces02:04

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Protein Networks02:26

Protein Networks

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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,...
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Protein Networks02:26

Protein Networks

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Protein-Drug Binding: Mechanism and Kinetics01:16

Protein-Drug Binding: Mechanism and Kinetics

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Protein-drug binding refers to the interaction between drugs and proteins within the body. This binding process can occur intracellularly, involving drug interactions with enzymes or receptors within cells, or extracellularly, involving plasma proteins in the blood.
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Protein Organization01:24

Protein Organization

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Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....
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Updated: Mar 31, 2026

Identifying Protein-protein Interaction Sites Using Peptide Arrays
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Identifying Protein-protein Interaction Sites Using Peptide Arrays

Published on: November 18, 2014

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New Compound Classes: Protein-Protein Interactions.

C Ottmann

    Handbook of Experimental Pharmacology
    |October 23, 2015
    PubMed
    Summary
    This summary is machine-generated.

    Targeting protein-protein interactions (PPIs) offers a vast new frontier for drug discovery, potentially expanding the druggable genome. Research highlights successful inhibition and stabilization of PPIs, encouraging further investment in this therapeutic area.

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    Area of Science:

    • Biochemistry
    • Pharmacology
    • Drug Discovery

    Background:

    • Protein-protein interactions (PPIs) are crucial in human physiology, with estimates of 300,000-650,000 interactions.
    • Modulating PPIs offers a promising strategy to expand the range of treatable diseases by targeting the

    Purpose of the Study:

    • To review examples of PPI inhibition and stabilization.
    • To discuss technologies used for identifying PPI targets.

    Main Methods:

    • Review of existing literature on small-molecule PPI inhibitors.
    • Analysis of natural products for PPI stabilization.
    • Examination of technologies for PPI identification.

    Main Results:

    • Numerous PPIs represent potential drug targets across various diseases.
    • Successful examples of both PPI inhibition and stabilization have been documented.
    • Various technologies facilitate the identification of druggable PPIs.

    Conclusions:

    • Targeted modulation of PPIs significantly broadens the scope of drug discovery.
    • Success stories in PPI modulation encourage further academic and industrial investment.
    • PPI modulators represent a generally applicable therapeutic technology.