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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...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
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

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Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly
09:34

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Published on: February 6, 2020

Cooperativity in macromolecular assembly.

James R Williamson1

  • 1Department of Molecular Biology, Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA. jrwill@scripps.edu

Nature Chemical Biology
|July 22, 2008
PubMed
Summary
This summary is machine-generated.

Cooperativity, a thermodynamic principle, drives macromolecular machine assembly. Understanding these interactions is key to deciphering complex biological machinery assembly and function.

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Last Updated: Jul 3, 2026

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Published on: February 6, 2020

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Area of Science:

  • Thermodynamics
  • Biophysical Chemistry
  • Molecular Biology

Background:

  • Macromolecular machines are essential for cellular functions.
  • The assembly and disassembly of these complexes are complex processes.
  • Understanding the underlying mechanisms is crucial but challenging.

Purpose of the Study:

  • To explore the role of thermodynamic cooperativity in driving the formation of specific macromolecular complexes.
  • To provide insights into the mechanisms governing the assembly and disassembly of multicomponent complexes.
  • To address the gap in understanding assembly mechanisms compared to structure and function.

Main Methods:

  • Thermodynamic analysis of intermolecular interactions.
  • Kinetic studies of complex formation.
  • Investigating cooperativity in macromolecular assembly.

Main Results:

  • Cooperativity is a key thermodynamic principle governing specific macromolecular complex formation.
  • Insights into the mechanisms of assembly and disassembly of multicomponent complexes were gained.
  • Challenges in understanding the thermodynamics and kinetics of intermolecular interactions were highlighted.

Conclusions:

  • Thermodynamic cooperativity is fundamental to the assembly of macromolecular machines.
  • Further research into the thermodynamics and kinetics of intermolecular interactions is needed.
  • Bridging the gap between understanding complex structure/function and their assembly mechanisms is essential.