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

7.4K
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...
7.4K
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

16.0K
In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
16.0K
ATP Synthase: Structure01:18

ATP Synthase: Structure

16.3K
ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
16.3K
ATP Driven Pumps II: P-type Pumps01:34

ATP Driven Pumps II: P-type Pumps

5.2K
The P-type pumps are a large family of integral membrane transporter ATPases. They are divided into five major types based on substrate specificity, from I to V.
A typical P-type pump has three cytosolic domains: nucleotide-binding (N), phosphorylation (P), and activator (A) domains. These domains are connected to the membrane-spanning helices by short amino acid segments. ATP hydrolysis and covalent phosphoenzyme intermediate formation are crucial parts of the catalytic cycle. At the highly...
5.2K
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

4.9K
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...
4.9K
Electron Transport Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

6.8K
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...
6.8K

También podría leer

Artículos Relacionados

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

Ordenar por
Same author

A detailed molecular picture of protein folding during active translation.

bioRxiv : the preprint server for biology·2026
Same author

How proteins fold.

Nature reviews. Molecular cell biology·2026
Same author

Morphological and molecular evidence of the Antarctic sleeper shark <i>Somniosus antarcticus</i> (Somniosidae) in northern Chile.

PeerJ·2026
Same author

Single-Molecule methods to investigate mechanisms of transcription by RNA polymerase of Mycobacterium tuberculosis.

Methods (San Diego, Calif.)·2026
Same author

SmartTrap: automated precision experiments with optical tweezers.

Nature methods·2026
Same author

The Rossmann2×2 Fold Attains its Native Structure Via a Defined Pathway of Sequential and Cooperative Folding Units.

bioRxiv : the preprint server for biology·2026

Video Experimental Relacionado

Updated: May 5, 2026

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
10:39

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

Published on: September 14, 2014

33.9K

La coordinación intersubunitaria en un anillo homomérico de la ATPasa.

Jeffrey R Moffitt1, Yann R Chemla, K Aathavan

  • 1Department of Physics and Jason L. Choy Laboratory of Single Molecule Biophysics, University of California, Berkeley, California 94720, USA.

Nature
|January 9, 2009
PubMed
Resumen

Los investigadores observaron directamente el motor de envasado de ADN del bacteriófago phi29, una ATPasa de anillo. Descubrieron que empaqueta el ADN en pasos coordinados de 2,5 pares de bases, totalizando 10 pares de bases por ciclo, revelando un nuevo mecanismo de coordinación.

Más Videos Relacionados

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
09:57

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach

Published on: December 17, 2016

6.1K
Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
12:07

Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET

Published on: October 9, 2021

2.6K

Videos de Experimentos Relacionados

Last Updated: May 5, 2026

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
10:39

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

Published on: September 14, 2014

33.9K
Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
09:57

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach

Published on: December 17, 2016

6.1K
Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
12:07

Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET

Published on: October 9, 2021

2.6K

Área de la Ciencia:

  • La bioquímica es la bioquímica.
  • Biología Molecular Biología Molecular
  • Biología Estructural Biología estructural.

Sus antecedentes:

  • Las ATPasas de anillo homomérico son motores moleculares cruciales involucrados en diversos procesos celulares.
  • La comprensión de sus mecanismos, en particular la coordinación intersubunidad y el tamaño del paso, es clave para aclarar sus funciones.

Objetivo del estudio:

  • Para observar directamente y cuantificar la coordinación intersubunitaria y el tamaño del paso del motor de envasado de ADN del bacteriófago phi29.
  • Para investigar el mecanismo de la translocación del ADN a nivel de una sola molécula.

Principales métodos:

  • Utilizó pinzas ópticas de alta resolución para aplicar fuerza y medir los movimientos precisos del motor phi29.
  • Realizó un análisis estadístico de los tiempos de permanencia y aplicó una gran fuerza para resolver los pasos individuales.

Principales resultados:

  • Envasado de ADN observado en incrementos discretos de 10 pares de bases (bp).
  • Se reveló que cada incremento de 10 pb se compone de cuatro pasos coordinados de 2,5 pb.
  • Se demostró que múltiples moléculas de ATP se unen e hidrolizan durante cada embalaje.

Conclusiones:

  • El motor phi29 exhibe un ciclo de hidrólisis altamente coordinado entre sus subunidades, un nuevo mecanismo para las ATPasas de anillo.
  • El tamaño del paso no entero requiere el desarrollo de nuevos modelos para las interacciones motor-ADN.