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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...

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:

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:

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,...

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Related Experiment Video

Updated: Jun 18, 2026

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

Supramolecular interactions between library members modulate the behavior of dynamic combinatorial libraries.

A Gastón Orrillo¹, Ricardo L E Furlan

¹Farmacognosia, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Rosario, Argentina.

The Journal of Organic Chemistry

|December 5, 2009

Summary

Supramolecular interactions within covalent dynamic combinatorial libraries (DCLs) significantly alter library responses to templates. These networks impact both the extent and precision of the library's reaction, even with identical molecular makeup.

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Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

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

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Published on: August 2, 2012

Area of Science:

Chemistry
Chemical Dynamics
Supramolecular Chemistry

Background:

Covalent dynamic combinatorial libraries (DCLs) are systems where molecular components reversibly form covalent bonds.
The behavior of DCLs can be influenced by non-covalent interactions between library members.
Understanding these interactions is crucial for controlling DCL responses.

Purpose of the Study:

To investigate the impact of supramolecular interactions on the response of DCLs to template molecules.
To determine how these interactions affect the degree and selectivity of the library's reaction.

Main Methods:

Utilized numerical simulations to model DCL behavior.
Analyzed the influence of inter-component supramolecular networks on library responses.

Main Results:

Demonstrated that supramolecular interactions significantly affect DCL responses.
Showed that these interactions influence both the magnitude and specificity of the library's reaction to a template.
Identified that even libraries with identical molecular compositions can exhibit different responses due to varying supramolecular networks.

Conclusions:

Supramolecular networks are a critical factor in dictating the functional output of DCLs.
Controlling supramolecular interactions offers a pathway to fine-tune the selectivity and degree of DCL responses.
This finding has implications for the design and application of DCLs in various fields.