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Videos de Conceptos Relacionados

Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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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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Allosteric Regulation01:08

Allosteric Regulation

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Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
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Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

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Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
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Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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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...
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The Two-State Receptor Model01:29

The Two-State Receptor Model

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The two-state receptor model explains a drug's interaction with receptors, such as G protein-coupled receptors and ligand-gated ion channels, to induce or inhibit a biological response. When no natural ligands are present, a receptor exists in an equilibrium of inactive (Ri) and active (Ra) conformations. The inactive form does not produce a response, while the active form generates a basal effect known as constitutive activity.
The binding affinity of a drug determines its interaction with...
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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
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Updated: Jul 19, 2025

Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells
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Programación de la Comunicación Química: Allostery frente al Mecanismo Multivalente

Dominic Lauzon1, Alexis Vallée-Bélisle1

  • 1Département de Chimie, Laboratoire de Biosenseurs et Nanomachines, Université de Montréal, Montréal QC H2V 0B3, Canada.

Journal of the American Chemical Society
|August 15, 2023
PubMed
Resumen

Los investigadores diseñaron un interruptor molecular basado en el ADN controlado por activadores multivalentes o alostéricos. La activación multivalente ofrece una mayor versatilidad en la sintonización de las propiedades del interruptor, aplicaciones prometedoras en biosensing y biología sintética.

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Área de la Ciencia:

  • La bioquímica
  • Biología molecular
  • Biología sintética

Sus antecedentes:

  • El surgimiento de la vida depende de la comunicación química y la integración de las entradas en las salidas.
  • La naturaleza utiliza la alostería y la activación multivalente para la integración de señales.
  • Allostery es bien entendido para la optimización de interruptores moleculares, pero la activación multivalente es menos entendida.

Objetivo del estudio:

  • Comparar la base termodinámica y los principios de diseño de la activación alostérica y multivalente.
  • Para diseñar un interruptor molecular basado en el ADN programable.
  • Investigar la sintonizabilidad de los interruptores moleculares utilizando diferentes mecanismos de activación.

Principales métodos:

  • Diseñado un interruptor molecular basado en el ADN.
  • Activadores de ADN diseñados para mecanismos multivalentes y alostéricos.
  • Se analizó la afinidad de unión, el rango dinámico y la vida media activada.

Principales resultados:

  • Se ha demostrado un interruptor programable basado en el ADN activado por activadores de ADN multivalentes o alostéricos.
  • Se demostró que la activación multivalente permite una programación más versátil de la afinidad del interruptor, el rango dinámico y la vida media en comparación con la activación alosterica.
  • Interfaces de unión diseñadas con precisión para activadores multivalentes.

Conclusiones:

  • El ensamblaje multivalente ofrece un enfoque simple y racional para ajustar las propiedades del interruptor molecular.
  • Este mecanismo proporciona una mayor versatilidad que la activación alostérica para controlar los interruptores moleculares.
  • Las aplicaciones potenciales incluyen biosensing, administración de fármacos, biología sintética y computación molecular.