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Cooperative Allosteric Transitions

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 Transitions

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 Transitions

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 Regulators

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 Regulators

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 Strength

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: May 16, 2026

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

Published on: July 17, 2019

Cooperativity in self-limiting equilibrium self-associating systems.

¹James Franck Institute and Department of Chemistry, University of Chicago, Chicago, Illinois 60637, USA.

The Journal of Chemical Physics

|December 5, 2012

Summary

This summary is machine-generated.

This study introduces a general thermodynamic theory for cooperative self-assembly, explaining how units form clusters with a specific size distribution. The minimal Flory-Huggins model provides a mechanism for this complex biological and synthetic process.

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Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

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Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates

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Published on: January 5, 2024

Area of Science:

Thermodynamics
Physical Chemistry
Biophysics

Background:

Cooperative self-assembly is common in biological and synthetic systems, forming clusters with specific size distributions.
Existing models are specific (e.g., viral capsids, micelles) and lack a general thermodynamic mechanism for double-peaked size distributions.
A general theory is needed to describe equilibrium assembly with peaks at monomer and large cluster sizes.

Purpose of the Study:

To develop a general thermodynamic mechanism for highly cooperative self-assembly processes.
To model systems exhibiting double-peaked size distributions (monomers and large clusters).
To provide a minimal Flory-Huggins type theory applicable to diverse self-assembly phenomena.

Main Methods:

Developed a minimal Flory-Huggins type theory for self-assembly.
Modified a non-cooperative free association model to allow favorable growth for intermediate cluster sizes.
Computed phase diagrams and mass distributions for self-assembly under temperature changes.

Main Results:

The new theory provides a general mechanism for cooperative self-assembly with double-peaked size distributions.
The model successfully describes equilibrium assembly, including the formation of large clusters and free monomers.
Phase diagrams illustrate self-assembly behavior upon cooling or heating, alongside mass distribution analysis.

Conclusions:

The developed Flory-Huggins type theory offers a general thermodynamic framework for cooperative self-assembly.
This model explains the characteristic double-peaked size distribution observed in many biological and synthetic systems.
The theory's applicability is demonstrated through phase diagram and mass distribution computations.