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Videos de Conceptos Relacionados

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...
Ligand Binding Sites02:40

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 Sites02:40

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 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...

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Video Experimental Relacionado

Updated: Jun 2, 2026

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
10:17

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

Published on: January 14, 2020

Mejorar la afinidad de unión por la cooperatividad entre la conformación del huésped y las interacciones

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
PubMed
Resumen

Las grandes moléculas de foldamer con grupos funcionales de glutamato muestran una alta afinidad de unión para varios huéspedes, incluidos los iones metálicos y las aminas. Los cambios conformacionales cooperativos, en lugar de estructuras rígidas, son la clave para este reconocimiento molecular mejorado.

Videos de Experimentos Relacionados

Last Updated: Jun 2, 2026

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
10:17

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

Published on: January 14, 2020

Área de la Ciencia:

  • Química supramolecular de las moléculas.
  • Biología Química Biología química.
  • Ciencia de los materiales Ciencia de los materiales.

Sus antecedentes:

  • El diseño de receptores sintéticos con altas afinidades de unión es un desafío significativo en el reconocimiento molecular.
  • Los pliegues de oligocolatos ofrecen un andamio versátil para crear arquitecturas moleculares complejas.
  • Comprender el papel de la dinámica conformacional en las interacciones huésped-invitado es crucial para optimizar las afinidades de unión.

Objetivo del estudio:

  • Para investigar las capacidades de unión de los foldameros oligocolatos funcionalizados con glutamato.
  • Para dilucidar la relación entre la conformación del huésped y la afinidad de unión del huésped.
  • Explorar el potencial de los cambios conformacionales cooperativos para mejorar el reconocimiento molecular.

Principales métodos:

  • Síntesis de foldameres de oligocolatos funcionalizados con glutamato.
  • Estudios de vinculación con varios huéspedes, incluidos los compuestos de Zn(OAc)(2), guanidina y amina.
  • Análisis de los cambios conformacionales del huésped utilizando métodos espectroscópicos y computacionales.

Principales resultados:

  • Los Foldamers demostraron altas afinidades de unión para los huéspedes Zn(OAc)(2), guanidina y amina.
  • Los cambios de conformación en los huéspedes del foldamer fueron esenciales para las altas afinidades observadas.
  • La cooperación más fuerte entre la conformación y la unión del huésped se produjo cerca del punto de transición plegado-despliegue.

Conclusiones:

  • Los foldameros oligocolatos funcionalizados con glutamato son huéspedes efectivos para el reconocimiento molecular.
  • Los cambios conformacionales cooperativos juegan un papel crítico en el logro de altas afinidades vinculantes.
  • Los huéspedes grandes y flexibles con cambios conformacionales cooperativos significativos pueden ser superiores a los huéspedes rígidos y preorganizados para el reconocimiento molecular.