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Related Concept Videos

Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Ligand Binding and Linkage00:49

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...
Ligand Binding and Linkage00:49

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...
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...

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Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors
10:33

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Published on: October 26, 2015

Crescent oligoamides as hosts: conformation-dependent binding specificity.

Kazuhiro Yamato1, Lihua Yuan, Wen Feng

  • 1Department of Chemistry, Natural Sciences Complex, University at Buffalo, The State University of New York, Buffalo, NY 14260, USA.

Organic & Biomolecular Chemistry
|August 27, 2009
PubMed
Summary
This summary is machine-generated.

Crescent oligoamides demonstrate high specificity and affinity for binding substituted guanidinium ions. This molecular recognition capability is crucial for developing advanced sensing and separation technologies.

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Area of Science:

  • Supramolecular Chemistry
  • Organic Chemistry

Background:

  • Guanidinium ions are important in biological systems and chemical processes.
  • Designing molecules for selective ion binding is a significant challenge.

Purpose of the Study:

  • To investigate the binding properties of crescent oligoamides.
  • To determine the specificity and affinity of these compounds for substituted guanidinium ions.

Main Methods:

  • Synthesis of crescent oligoamide derivatives.
  • Binding studies using techniques such as Nuclear Magnetic Resonance (NMR) spectroscopy and Isothermal Titration Calorimetry (ITC).

Main Results:

  • Crescent oligoamides exhibit strong binding to substituted guanidinium ions.
  • High selectivity was observed, with minimal binding to other cationic species.
  • Affinity constants indicate robust molecular recognition.

Conclusions:

  • Crescent oligoamides are effective hosts for substituted guanidinium ions.
  • The unique structure of crescent oligoamides facilitates specific ion recognition.
  • These findings open avenues for applications in molecular sensing and ion separation.