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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...
Molecular Models02:00

Molecular Models

Physical models representing molecular architectures of chemical compounds play essential roles in understanding chemistry. The use of molecular models makes it easier to visualize the structures and shapes of atoms and molecules.
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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Related Experiment Video

Updated: Jun 12, 2026

Structure-Based Simulation and Sampling of Transcription Factor Protein Movements along DNA from Atomic-Scale Stepping to Coarse-Grained Diffusion
09:17

Structure-Based Simulation and Sampling of Transcription Factor Protein Movements along DNA from Atomic-Scale Stepping to Coarse-Grained Diffusion

Published on: March 1, 2022

Towards modeling molecular cooperativity on the cellular scale.

F N Braun1

  • 1University of Tromsø, Norway. f.n.braun@gmail.com

Biophysical Chemistry
|June 1, 2010
PubMed
Summary
This summary is machine-generated.

Molecular cooperativity, originally for protein folding, now describes cellular organization. This framework explains cytoplasmic phase separation and ribosome partitioning, impacting cellular evolution.

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Last Updated: Jun 12, 2026

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Area of Science:

  • Cellular Biology
  • Statistical Mechanics
  • Biophysics

Background:

  • Molecular cooperativity explains protein folding and ligand binding kinetics and thermodynamics.
  • Extrapolating this concept to the cellular scale offers new insights into cytological organization.

Purpose of the Study:

  • To explore molecular cooperativity as a thermally driven mode of cellular organization.
  • To apply the equation of state (EOS) framework to understand cytoplasmic phenomena.
  • To investigate ribosome partitioning during phase separation.

Main Methods:

  • Utilizing classical statistical mechanics and the equation of state (EOS) framework.
  • Analyzing cytoplasmic phase separation and gelation phenomena.
  • Thermodynamic modeling of ribosome partitioning.

Main Results:

  • A unified EOS account of cytoplasmic phase separation and gelation was established, highlighting osmoregulatory control.
  • Spontaneous thermodynamic partitioning of ribosomes was demonstrated during phase separation.
  • This partitioning suggests a potential translation-transcription decoupling.

Conclusions:

  • The equation of state framework provides a unified view of cytoplasmic organization phenomena.
  • Ribosome partitioning during phase separation has significant implications for cellular evolution.
  • The concept of molecular cooperativity is a powerful tool for understanding cellular organization and function.