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Related Concept Videos

Protein Networks02:26

Protein Networks

4.1K
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-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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Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

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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.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
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Ligand Binding Sites02:40

Ligand Binding Sites

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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.
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...
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Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

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Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
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Gene Families01:57

Gene Families

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Gene families consist of groups of genes proposed to have originated from a common ancestor. Typically these arise through events in which a gene or genes are mistakenly duplicated during cell division. Unlike their parent genes (which are subject to selection pressure to maintain function), these gene copies do not need to preserve their sequences and may evolve at a relatively faster rate.
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...
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The IntAct database: efficient access to fine-grained molecular interaction data.

Noemi Del Toro1, Anjali Shrivastava1, Eliot Ragueneau1

  • 1European Bioinformatics Institute (EMBL-EBI), European Molecular Biology Laboratory, Hinxton, Cambridgeshire CB10 1SD, UK.

Nucleic Acids Research
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Summary
This summary is machine-generated.

The IntAct molecular interaction database now offers over one million curated protein interactions. Its enhanced website provides a user-friendly platform for detailed molecular interaction data exploration.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Bioinformatics

Background:

  • The IntAct molecular interaction database is a key resource for curated protein-protein interactions.
  • It aggregates data from scientific literature and direct submissions, supported by the International Molecular Exchange (IMEx) consortium.
  • Accurate curation is vital for interpreting molecular interaction data.

Purpose of the Study:

  • To present recent advancements in IntAct's curation efforts.
  • To introduce a redeveloped, more user-friendly IntAct website.
  • To improve the accessibility and detail of molecular interaction data.

Main Methods:

  • Curating molecular interactions from scientific literature and direct depositions.
  • Implementing a fine-grained data and curation model for experimental detail.
  • Redeveloping the IntAct website for enhanced user experience.

Main Results:

  • As of August 2021, IntAct contains over one million binary interactions.
  • Data is curated by twelve global partners of the IMEx consortium.
  • A new website offers a more detailed and user-friendly presentation of IntAct data.

Conclusions:

  • IntAct continues to be a vital, expanding resource for molecular interaction data.
  • The database's commitment to detailed curation ensures data quality and interpretability.
  • The website redevelopment enhances data accessibility for researchers.