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

Ligand Binding and Linkage00:49

Ligand Binding and Linkage

5.3K
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...
5.3K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

8.4K
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...
8.4K
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

6.3K
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...
6.3K
Electron Transport Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

8.7K
During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
8.7K
Colors and Magnetism03:02

Colors and Magnetism

13.1K
Color in Coordination Complexes
When atoms or molecules absorb light at the proper frequency, their electrons are excited to higher-energy orbitals. For many main group atoms and molecules, the absorbed photons are in the ultraviolet range of the electromagnetic spectrum, which cannot be detected by the human eye. For coordination compounds, the energy difference between the d orbitals often allows photons in the visible range to be absorbed and emitted, which is seen as colors by the human...
13.1K

También podría leer

Artículos Relacionados

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

Ordenar por
Same author

Tracking the Early Hydration Reaction of Cementitious Calcium Silicate Hydrate via DNP-Enhanced Solid-State NMR.

Journal of the American Chemical Society·2026
Same author

Mapping mRNA Localization and Internal Structure in Lipid Nanoparticles through Solid-State Dynamic Nuclear Polarization NMR and Proton Spin-Diffusion Modeling.

Small methods·2026
Same author

A Rigid Supramolecular Solution to a Flexible Problem: A Multifunctional Calix[4]arene-Based Strategy to Prevent α‑Synuclein Toxicity.

ACS central science·2026
Same author

Electronic Structures of Pt(0) Complexes and Atomically Precise Clusters from Solid-State <sup>195</sup>Pt NMR Signatures.

Journal of the American Chemical Society·2026
Same author

In Situ Light-Induced Degradation of Hybrid Perovskites by NMR Spectroscopy.

Journal of the American Chemical Society·2026
Same author

Fluorinated Biradicals for <sup>19</sup>F Magic-Angle Spinning Dynamic Nuclear Polarization-Enhanced NMR Spectroscopy.

Journal of the American Chemical Society·2026

Video Experimental Relacionado

Updated: Dec 1, 2025

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides
11:04

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

Published on: September 7, 2019

9.6K

Respuesta multimodal al enlace de cobre en la dinámica de la superóxido dismutasa

Marta Bonaccorsi1, Michael J Knight1, Tanguy Le Marchand1

  • 1Centre de RMN à Très Hauts Champs, FRE 2034 (CNRS/Université Claude Bernard Lyon 1/Ecole Normale Supérieure de Lyon), University of Lyon, 69100 Villeurbanne, France.

Journal of the American Chemical Society
|November 9, 2020
PubMed
Resumen

Se estudió la dinámica de la superóxido de cobre/zinco dismutasa (SOD) en dos formas metalizadas. La absorción de iones metálicos modula la flexibilidad de las proteínas, influyendo en el movimiento a través de varias escalas de tiempo.

Más Videos Relacionados

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

9.9K
Quantifying the Binding Interactions Between CuII and Peptide Residues in the Presence and Absence of Chromophores
11:38

Quantifying the Binding Interactions Between CuII and Peptide Residues in the Presence and Absence of Chromophores

Published on: April 5, 2022

2.8K

Videos de Experimentos Relacionados

Last Updated: Dec 1, 2025

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides
11:04

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

Published on: September 7, 2019

9.6K
Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

9.9K
Quantifying the Binding Interactions Between CuII and Peptide Residues in the Presence and Absence of Chromophores
11:38

Quantifying the Binding Interactions Between CuII and Peptide Residues in the Presence and Absence of Chromophores

Published on: April 5, 2022

2.8K

Área de la Ciencia:

  • La bioquímica
  • La biofísica
  • Biología estructural

Sus antecedentes:

  • La superóxido de cobre y zinc dismutasa (SOD) es una metalenzima crucial implicada en la esclerosis lateral amiotrófica.
  • La comprensión de la relación estructura-función de SOD es vital para la investigación de enfermedades neurodegenerativas.

Objetivo del estudio:

  • Investigar el impacto de la metalización en la dinámica de la SOD.
  • Para cuantificar los movimientos de proteínas en diferentes estados metalizados de SOD.

Principales métodos:

  • Espectroscopia de resonancia magnética nuclear (RMN) en estado sólido.
  • Giro de ángulo mágico rápido (MAS) en campos magnéticos altos (800-1000 MHz).
  • Análisis de las preparaciones microcristalinas de Cu,Zn-SOD y E,Zn-SOD.

Principales resultados:

  • La absorción de iones metálicos no rigidifica el SOD, sino que redistribuye los procesos de movimiento.
  • Los movimientos se cuantificaron en un rango dinámico de nanosegundos a milisegundos.
  • Se observó un acoplamiento entre la dinámica de la cadena lateral de histidina y los elementos remotos de la columna vertebral.

Conclusiones:

  • El estado de metalización influye significativamente en el paisaje dinámico de SOD.
  • La flexibilidad de SOD está afinada por la incorporación de iones metálicos, lo que afecta la función de las proteínas.
  • Estos hallazgos ofrecen información sobre el papel de SOD en los mecanismos de la enfermedad.