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Related Concept Videos

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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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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The Equilibrium Binding Constant and Binding Strength

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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: Jul 6, 2025

Mapping the Binding Site of an Aptamer on ATP Using MicroScale Thermophoresis
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AptaDB: a comprehensive database integrating aptamer-target interactions.

Long Chen1, Zhuohang Yu1, Zengrui Wu1

  • 1Shanghai Frontiers Science Center of Optogenetic Techniques for Cell Metabolism, Shanghai Key Laboratory of New Drug Design, School of Pharmacy, East China University of Science and Technology, Shanghai 200237, China.

RNA (New York, N.Y.)
|January 2, 2024
PubMed
Summary
This summary is machine-generated.

A new database, AptaDB, integrates diverse aptamer data, including interactions and properties. This resource supports computational aptamer design and screening, advancing pharmacology and medicine.

Keywords:
annotationaptamer–target interactiondatabasesimilar aptamers

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Area of Science:

  • Biotechnology
  • Bioinformatics
  • Computational Biology

Background:

  • Aptamers show great potential in pharmacology, medicine, and analytical chemistry.
  • Lack of integrated data hinders computational aptamer development and reuse.
  • Existing aptamer databases lack comprehensive, validated information.

Purpose of the Study:

  • To develop a comprehensive, public-access database for aptamer-related data.
  • To facilitate computational methods and aptamer reuse.
  • To provide a user-friendly resource for aptamer research.

Main Methods:

  • Manually collected and integrated experimentally validated data from literature.
  • Included six key data components: aptamer-target interactions, properties, structures, targets, experimental activity, and similar aptamers.
  • Developed a user-friendly interface for data access.

Main Results:

  • AptaDB contains 1350 aptamer-target interactions, 1230 binding affinity constants, and 1293 aptamer sequences.
  • Features twice the number of entries compared to existing aptamer databases.
  • Unique integration of diverse aptamer data categories.

Conclusions:

  • AptaDB offers a unique and comprehensive resource for aptamer research.
  • The database is expected to be a powerful tool for rational aptamer design and screening.
  • AptaDB will be continuously updated to reflect advancements in aptamer research.