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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

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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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Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
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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.
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DNA probes are fragments of DNA labeled with a reporter tag to enable their detection or purification. The resulting labeled DNA probes can then hybridize to target nucleic acid sequences through complementary base-pairing, and may be used to recover or identify these regions.
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Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
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Updated: Nov 21, 2025

Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics
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Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics

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Deciphering molecular interactions by proximity labeling.

Wei Qin1, Kelvin F Cho1,2, Peter E Cavanagh3

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This summary is machine-generated.

Proximity labeling (PL) tags proteins interacting with a specific

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Area of Science:

  • Molecular biology
  • Biochemistry
  • Cell biology

Background:

  • Biological processes rely on molecular interactions.
  • Proximity labeling (PL) tags endogenous interaction partners of specific protein 'baits'.
  • This technology utilizes promiscuous enzymes to generate reactive species in living cells.

Purpose of the Study:

  • Review the development of proximity labeling technologies.
  • Highlight studies applying PL for molecular interaction discovery.
  • Focus on mapping protein-protein, protein-RNA, and protein-DNA interactions.

Main Methods:

  • Genetic fusion of proteins to promiscuous enzymes.
  • Catalysis of diffusible reactive species generation.
  • Enrichment and identification of tagged molecules via mass spectrometry or sequencing.

Main Results:

  • PL enables the discovery of endogenous molecular interactions.
  • Successful mapping of protein-protein interactions.
  • Successful mapping of protein-RNA and protein-DNA interactions.

Conclusions:

  • Proximity labeling is a powerful tool for studying molecular interactions.
  • PL facilitates the analysis of complex biological networks in living systems.
  • This technology is applicable in diverse biological contexts, including whole organisms.