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Related Concept Videos

Cooperative Allosteric Transitions01:58

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

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

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 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...
The Equilibrium Binding Constant and Binding Strength02:18

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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Related Experiment Video

Updated: Jun 26, 2026

Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation
07:57

Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation

Published on: August 21, 2019

Information theoretical quantification of cooperativity in signalling complexes.

Tom Lenaerts1, Jesper Ferkinghoff-Borg, Joost Schymkowitz

  • 1SWITCH, VIB, Brussels, Belgium. tlenaert@vub.ac.be

BMC Systems Biology
|January 20, 2009
PubMed
Summary

This study demonstrates how Shannon information quantifies cellular information exchange and protein complex cooperativity. It reveals optimal protein concentrations for effective biological system switching and signaling.

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Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation
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Area of Science:

  • Biophysics
  • Systems Biology
  • Molecular Biology

Background:

  • Intracellular information exchange via signaling proteins is crucial for cell function and survival.
  • Mapping protein interactomes and understanding molecular cooperativity enable formalizing biological information.
  • Formalizing information in diverse biological contexts is now feasible.

Purpose of the Study:

  • To demonstrate Shannon's mutual information as a quantitative measure for biological information exchange.
  • To analyze cooperativity in macromolecular complex assembly using an information-theoretic approach.
  • To link classical thermodynamics to information exchange for understanding cellular processes.

Main Methods:

  • Utilizing Shannon's mutual information to quantify information in biological systems.
  • Modeling protein complexes as noisy communication channels.
  • Applying equilibrium thermodynamic quantities (binding affinities, chemical potentials) to quantify information and engineering properties.

Main Results:

  • Shannon's mutual information quantifies information exchange and cooperativity in macromolecular complexes.
  • Protein complexes function as noisy communication channels.
  • Thermodynamic quantities quantify information exchange, channel noise, and capacity, identifying optimal protein concentrations for system switching.

Conclusions:

  • A novel framework analyzes cooperativity in macromolecular complexes using information theory.
  • Identifies conditions (protein concentrations) for maximal information exchange and system effectiveness.
  • Enables direct analysis of biological qualities like sensitivity, robustness, and plasticity via information exchange, offering an intuitive visualization of network cooperativity.