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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...

Ligand Binding Sites

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...

Ligand Binding Sites

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...

Ligand Binding and Linkage

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked. In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...

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Related Experiment Video

Updated: Jun 2, 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

Enhancing binding affinity by the cooperativity between host conformation and host-guest interactions.

Zhenqi Zhong¹, Xueshu Li, Yan Zhao

¹Department of Chemistry, Iowa State University, Ames, Iowa 50011-3111, USA.

Journal of the American Chemical Society

|May 18, 2011

Summary

This summary is machine-generated.

Large foldamer molecules with glutamate functional groups show high binding affinity for various guests, including metal ions and amines. Cooperative conformational changes, rather than rigid structures, are key to this enhanced molecular recognition.

Related Experiment Videos

Last Updated: Jun 2, 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

Area of Science:

Supramolecular Chemistry
Chemical Biology
Materials Science

Background:

Designing synthetic receptors with high binding affinities is a significant challenge in molecular recognition.
Oligocholate foldamers offer a versatile scaffold for creating complex molecular architectures.
Understanding the role of conformational dynamics in host-guest interactions is crucial for optimizing binding affinities.

Purpose of the Study:

To investigate the binding capabilities of glutamate-functionalized oligocholate foldamers.
To elucidate the relationship between host conformation and guest-binding affinity.
To explore the potential of cooperative conformational changes in enhancing molecular recognition.

Main Methods:

Synthesis of glutamate-functionalized oligocholate foldamers.
Binding studies with various guests, including Zn(OAc)(2), guanidine, and amine compounds.
Analysis of host conformational changes using spectroscopic and computational methods.

Main Results:

Foldamers demonstrated high binding affinities for Zn(OAc)(2), guanidine, and amine guests.
Conformational changes in the foldamer hosts were essential for the observed high affinities.
Strongest cooperativity between conformation and guest binding occurred near the folding-unfolding transition point.

Conclusions:

Glutamate-functionalized oligocholate foldamers are effective hosts for molecular recognition.
Cooperative conformational changes play a critical role in achieving high binding affinities.
Large, flexible hosts with significant cooperative conformational changes may be superior to rigid, preorganized hosts for molecular recognition.