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Related Concept Videos

Ligand Binding Sites02:40

Ligand Binding Sites

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.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Ligand Binding Sites02:40

Ligand Binding Sites

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.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
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...
Molecular Models02:00

Molecular Models

Physical models representing molecular architectures of chemical compounds play essential roles in understanding chemistry. The use of molecular models makes it easier to visualize the structures and shapes of atoms and molecules.
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:

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Updated: Jun 18, 2026

New Features in Visual Dynamics 3.0
05:00

New Features in Visual Dynamics 3.0

Published on: August 9, 2024

MINT, the molecular interaction database: 2009 update.

Arnaud Ceol1, Andrew Chatr Aryamontri, Luana Licata

  • 1Department of Biology, University of Rome Tor Vergata, Via della Ricerca Scientifica, 00133 Rome. arnaud.ceol@uniroma2.it

Nucleic Acids Research
|November 10, 2009
PubMed
Summary
This summary is machine-generated.

The Molecular Interactions (MINT) database has expanded its molecular interaction data and improved its user interface. It now adheres to PSI-MI standards for better data analysis and accessibility.

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Area of Science:

  • Molecular Biology
  • Bioinformatics
  • Biochemistry

Background:

  • The Molecular Interactions (MINT) database serves as a public repository for molecular interactions.
  • Databases of molecular interactions are crucial for understanding cellular processes.
  • Previous versions of MINT have been reported in scientific literature.

Purpose of the Study:

  • To report on the recent growth and evolution of the MINT database.
  • To highlight improvements in MINT's scope, curation policy, and user interface.
  • To emphasize MINT's adoption of community standards for molecular interaction data.

Main Methods:

  • MINT collects data from peer-reviewed publications.
  • The database utilizes the Proteomics Standards Initiative-Molecular Interaction (PSI-MI) standards for annotation and representation.
  • MINT is part of the IMEx (Interaction database Exchange) consortium.

Main Results:

  • MINT has significantly increased in size since its last report.
  • The curation policy has been refined for greater precision.
  • An enhanced, user-friendly interface has been developed for easier data analysis.

Conclusions:

  • MINT has evolved to meet user requirements through enhanced data and usability.
  • Adherence to PSI-MI standards facilitates data integration and interoperability.
  • MINT's continued development supports the research community's need for comprehensive molecular interaction data.