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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...

Noncovalent Attractions in Biomolecules

Noncovalent Attractions in Biomolecules

Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...

Noncovalent Attractions in Biomolecules

Noncovalent Attractions in Biomolecules

Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...

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...

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Related Experiment Video

Updated: Jun 7, 2026

Controlling the Size, Shape and Stability of Supramolecular Polymers in Water

Controlling the Size, Shape and Stability of Supramolecular Polymers in Water

Published on: August 2, 2012

Supramolecular balance: using cooperativity to amplify weak interactions.

Mihaela Roman¹, Caroline Cannizzo, Thomas Pinault

¹Université Claude Bernard-Lyon 1, ICBMS-UMR 5246, 43 Boulevard du 11 Novembre 1918, F-69622 Villeurbanne cedex, France.

Journal of the American Chemical Society

|November 6, 2010

Summary

Researchers developed a sensitive method to detect subtle changes in weak supramolecular interactions. This technique uses a cooperative molecular platform and temperature scanning to reveal interaction differences as small as 60 J/mol.

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Area of Science:

Supramolecular Chemistry
Physical Chemistry
Chemical Biology

Background:

Precise characterization of weak supramolecular interactions is crucial for fields like catalysis, crystal engineering, ligand binding, and protein folding.
Current methods often lack the sensitivity to detect minor variations in these interactions in solution.

Purpose of the Study:

To develop a significantly more sensitive method for probing weak supramolecular interactions in solution.
To demonstrate the utility of a cooperative supramolecular platform for detecting subtle interaction energy differences.

Main Methods:

A combined theoretical and experimental approach was employed.
A supramolecular platform featuring a highly cooperative configurational transition was designed.
Temperature scanning experiments were used to monitor perturbations in the platform's transition upon molecular modification.

Main Results:

The developed method successfully detected interaction differences as low as 60 J/mol.
The platform's sensitivity allowed for the differentiation of steric repulsion effects (vinyl vs. alkyl groups) and solvation effects.

Conclusions:

A novel, highly sensitive method for studying weak supramolecular interactions in solution has been established.
The cooperative supramolecular platform approach offers a powerful tool for quantitative analysis of subtle intermolecular forces.
This technique has broad implications for understanding molecular recognition and self-assembly processes.