Related Experiment Video
Updated: Jun 13, 2026

14:37
Modeling an Enzyme Active Site using Molecular Visualization Freeware
Published on: December 25, 2021
The publication and database deposition of molecular interaction data
Sandra Orchard1, Bruno Aranda1, Henning Hermjakob1
1European Bioinformatics Institute, Wellcome Trust Genome Campus, Cambridge, United Kingdom.
Current Protocols in Protein Science
|April 16, 2010
Summary
Submitting molecular interaction data to public databases enhances data accessibility and visibility. This process, supported by curators and accession numbers, integrates seamlessly into manuscript preparation.
Area of Science:
- Molecular Biology
- Bioinformatics
- Data Science
Background:
- Public domain interaction databases are crucial for sharing molecular interaction data.
- Data sharing improves research reproducibility and accelerates scientific discovery.
- The International Molecular Exchange (IMEx) databases facilitate broad data dissemination.
Purpose of the Study:
- To outline protocols for submitting molecular interaction data to public databases.
- To emphasize the benefits of data deposition for researchers and the scientific community.
- To guide authors in integrating data submission into their manuscript preparation workflow.
Main Methods:
- Providing alternative protocols for data submission based on dataset size.
- Describing the process of obtaining accession numbers for pre-publication datasets.
- Detailing the use of controlled vocabulary for data standardization.
Main Results:
- Data deposition increases the quality, quantity, and visibility of molecular interaction information.
- Pre-publication submission with accession numbers enhances data accessibility in publications.
- Database curators offer assistance to ensure accurate data representation.
Conclusions:
- Integrating data submission into manuscript preparation is essential for maximizing research impact.
- Standardized data deposition practices improve data discoverability and usability.
- Public databases serve as vital resources for the molecular biology research community.
Related Concept Videos
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...
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-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 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,...
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,...
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:
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.
Noncovalent Attractions in Biomolecules
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,...
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,...
