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Related Concept Videos

Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form dimers that...
Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form dimers that...
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Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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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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Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
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Cooperative binding.

Melanie I Stefan1, Nicolas Le Novère

  • 1Division of Biology, California Institute of Technology, Pasadena, California, United States of America.

Plos Computational Biology
|July 12, 2013
PubMed
Summary
This summary is machine-generated.

Cooperative binding describes how molecules interact, influencing biological processes. This phenomenon, observed in proteins and nucleic acids, involves ligand concentration affecting binding site occupancy nonlinearly.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Molecular binding is the interaction leading to stable molecular associations.
  • Cooperative binding occurs when ligand binding to a macromolecule is a nonlinear function of ligand concentration.
  • This binding can be positive (supralinear) or negative (infralinear).

Purpose of the Study:

  • To define and explain the concept of cooperative binding.
  • To highlight the mechanisms and implications of cooperative binding in biological systems.
  • To underscore the significance of cooperative binding in various biochemical and physiological processes.

Main Methods:

  • The study defines cooperative binding based on the relationship between ligand concentration and occupied binding sites.
  • It explains the nonlinear function and affinity changes associated with this binding.
  • It provides examples in proteins and nucleic acids, such as transcription factors.

Main Results:

  • Cooperative binding is characterized by a nonlinear dependence of ligand-bound sites on ligand concentration.
  • This interaction can be modulated by changes in molecular affinity.
  • Positive and negative cooperativity represent distinct binding behaviors.

Conclusions:

  • Cooperative binding is a crucial mechanism in molecular interactions, particularly in proteins and nucleic acids.
  • It underlies a wide array of biochemical and physiological functions.
  • Understanding cooperativity is essential for comprehending complex biological systems.