Jove
Visualize
Contáctanos
JoVE
x logofacebook logolinkedin logoyoutube logo
ACERCA DE JoVE
Visión GeneralLiderazgoBlogCentro de Ayuda JoVE
AUTORES
Proceso de PublicaciónConsejo EditorialAlcance y PolíticasRevisión por ParesPreguntas FrecuentesEnviar
BIBLIOTECARIOS
TestimoniosSuscripcionesAccesoRecursosConsejo Asesor de BibliotecasPreguntas Frecuentes
INVESTIGACIÓN
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchivo
EDUCACIÓN
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualCentro de Recursos para ProfesoresSitio de Profesores
Términos y Condiciones de Uso
Política de Privacidad
Políticas

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...
Mutations in Microorganisms01:18

Mutations in Microorganisms

Mutations are heritable changes in an organism’s genome involving alterations in the base sequence of DNA or RNA. These changes can influence cellular processes and phenotypic traits, potentially transforming the unaltered wild type into a mutant form. Such changes, termed forward mutations, are pivotal in shaping the genetic diversity of organisms.RNA viruses exhibit the highest mutation rates due to the absence of robust proofreading mechanisms during genome replication. In contrast,...
The Equilibrium Binding Constant and Binding Strength02:18

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 Strength02:18

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:

También podría leer

Artículos Relacionados

Artículos vinculados a este trabajo por autores compartidos, revista y gráfico de citas.

Ordenar por
Same author

Tubulin State Determines Proteopathic Fate.

Cytoskeleton (Hoboken, N.J.)·2026
Same author

Modulation of Biomolecular Aggregate Morphology and Condensate Infectivity.

Biomolecules·2026
Same author

NANOG Proximity Proteomics Maps Neighborhood Hubs Linked to Mesenchymal Stem Cell Stemness and Chromatin Control.

Biomolecules·2026
Same author

Condensate State as Determinant of Amyloid Pathology in Neurodegeneration.

Biomolecules·2026
Same author

Multivalent weak contacts shape chaperone-nascent protein interactions.

bioRxiv : the preprint server for biology·2026
Same author

Label-Free Microfluidic Modulation Spectroscopy Monitors RNA Origami Structure and Stability.

Biosensors·2026

Video Experimental Relacionado

Updated: Jun 23, 2026

A Novel Saturation Mutagenesis Approach: Single Step Characterization of Regulatory Protein Binding Sites in RNA Using Phosphorothioates
11:49

A Novel Saturation Mutagenesis Approach: Single Step Characterization of Regulatory Protein Binding Sites in RNA Using Phosphorothioates

Published on: August 21, 2018

Caracterizar el papel de la modulación del conjunto en los cambios inducidos por mutación en la afinidad de unión.

Anthony Manson1, Steven T Whitten, Josephine C Ferreon

  • 1Department of Biochemistry and Molecular Biology, and Sealy Center for Structural Biology and Biophysics, University of Texas Medical Branch, Galveston, Texas 77555, USA.

Journal of the American Chemical Society
|April 29, 2009
PubMed
Resumen

Las fluctuaciones conformacionales de las proteínas son cruciales para las funciones biológicas como el reconocimiento molecular. Nuestro estudio muestra que el análisis de estas dinámicas, particularmente en los dominios SH3, predice con precisión las energías de unión y revela información sobre las interacciones proteína-ligando.

Más Videos Relacionados

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates
06:48

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates

Published on: January 5, 2024

Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells
15:28

Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells

Published on: October 1, 2010

Videos de Experimentos Relacionados

Last Updated: Jun 23, 2026

A Novel Saturation Mutagenesis Approach: Single Step Characterization of Regulatory Protein Binding Sites in RNA Using Phosphorothioates
11:49

A Novel Saturation Mutagenesis Approach: Single Step Characterization of Regulatory Protein Binding Sites in RNA Using Phosphorothioates

Published on: August 21, 2018

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates
06:48

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates

Published on: January 5, 2024

Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells
15:28

Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells

Published on: October 1, 2010

Área de la Ciencia:

  • Dinámica de las proteínas Dinámica de las proteínas.
  • Reconocimiento molecular de reconocimiento.
  • La biofísica es la biofísica.

Sus antecedentes:

  • Las fluctuaciones conformacionales de las proteínas son esenciales para los procesos biológicos.
  • Comprender estas dinámicas ayuda a comprender la catálisis enzimática, el reconocimiento molecular y la señalización alostérica.

Objetivo del estudio:

  • Para investigar el papel de las fluctuaciones conformacionales en el reconocimiento de sustrato/ligando.
  • Para analizar la reacción de unión entre un dominio SH3 y su péptido asociado.

Principales métodos:

  • Las fluctuaciones del dominio SH3 enumeradas usando un algoritmo de modelo de colisión de esfera dura.
  • Energéticas de enlace calculadas con una función de energía basada en la estructura.
  • Aplicó el análisis de coordenadas principales a conjuntos computarizados para caracterizar variaciones conformacionales.

Principales resultados:

  • Un modelo simple reprodujo con precisión los efectos de la mutación en las energías de unión de SH3.
  • Las fluctuaciones conformacionales en SH3, especialmente el bucle RT, son diversas y se aproximan por estados aleatorios.
  • Las diferencias en la afinidad de unión entre mutantes se correlacionan con cambios en los principales modos de variación conformacional.

Conclusiones:

  • Los bucles dinámicos de proteínas pueden acceder a una amplia gama de estados conformacionales.
  • Una comprensión completa del reconocimiento molecular requiere considerar la distribución completa de los estados de las proteínas.
  • Este enfoque proporciona información cuantitativa sobre las interacciones proteína-ligando.