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Related Concept Videos

Single-Strand DNA Binding Proteins01:03

Single-Strand DNA Binding Proteins

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For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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Conserved Binding Sites

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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
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The Equilibrium Binding Constant and Binding Strength02:18

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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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Related Experiment Video

Updated: Sep 5, 2025

Single-molecule Manipulation of G-quadruplexes by Magnetic Tweezers
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G4-quadruplex-binding proteins: review and insights into selectivity.

Vanessa Meier-Stephenson1,2,3

  • 1Department of Medicine, Division of Infectious Diseases, University of Alberta, Edmonton, AB Canada.

Biophysical Reviews
|July 6, 2022
PubMed
Summary

This review explores G-quadruplexes (G4Qs) and their binding proteins (G4BPs). It summarizes current literature on G4Q-G4BP interactions, focusing on binding modes and selectivity, to advance small-molecule drug development.

Keywords:
DNA–protein interactionsG4-quadruplexesQuadruplex-binding proteinsRNA–protein interactions

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Area of Science:

  • Genomics and Molecular Biology
  • Structural Biology
  • Drug Discovery

Background:

  • The human genome contains over 700,000 G-quadruplexes (G4Qs), primarily in regulatory regions.
  • G4Qs play crucial roles in cellular processes by interacting with cellular proteins.
  • Small molecules targeting G4Q-binding proteins (G4BPs) are a new area of drug development.

Purpose of the Study:

  • To review and summarize the current literature on G4Q-G4BP interactions.
  • To categorize G4BP binding modes and identify commonalities.
  • To highlight specific G4Q-G4BP interactions and address selectivity.

Main Methods:

  • Literature review of G4Q-G4BP interactions.
  • Categorization of binding modes.
  • Analysis of structural and interaction data.

Main Results:

  • G4Qs are prevalent in the human genome and involved in cellular regulation.
  • Cellular proteins (G4BPs) interact with G4Qs, influencing their function.
  • Limited high-resolution structural data exists for G4Q-G4BP interactions.

Conclusions:

  • Understanding G4Q-G4BP interactions is crucial for developing targeted therapeutics.
  • Further research is needed to elucidate G4BP selectivity and binding mechanisms.
  • This review provides a foundation for future studies in G4Q-based drug discovery.