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

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

18.2K
Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
18.2K
Protein Diffusion in the Membrane01:24

Protein Diffusion in the Membrane

4.6K
Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
4.6K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

18.5K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
18.5K
Protein Folding01:25

Protein Folding

8.7K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
8.7K
Protein-protein Interfaces02:04

Protein-protein Interfaces

13.3K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
13.3K
Ligand Binding Sites02:40

Ligand Binding Sites

13.2K
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...
13.2K

También podría leer

Artículos Relacionados

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

Ordenar por
Same author

Mapping and engineering the human cell-cell interactome.

Nature biotechnology·2026
Same author

Controlling metal-carbonate phase, form, and function through de novo protein design.

bioRxiv : the preprint server for biology·2026
Same author

Programmed synthesis of mesoporous protein crystals in cellular reactors.

Nature nanotechnology·2026
Same author

Generative design of programmable asymmetric β-barrel nanopores.

bioRxiv : the preprint server for biology·2026
Same author

Author Correction: De novo design of quasisymmetric two-component protein cages.

Nature·2026
Same author

De novo design of RNA pseudoknots with deep learning.

bioRxiv : the preprint server for biology·2026
Same journal

Retraction Note: NSD2 targeting reverses plasticity and drug resistance in prostate cancer.

Nature·2026
Same journal

Enhanced B cell priming induces broadly neutralizing HIV-1 apex antibodies.

Nature·2026
Same journal

Vaccination elicits HIV broadly neutralizing antibodies in primates.

Nature·2026
Same journal

Child online safety needs more than social-media bans.

Nature·2026
Same journal

Ebola preparedness must start with ecosystems and before humans show symptoms.

Nature·2026
Same journal

AI tools can speed up thinking, but evidence still comes from the lab bench.

Nature·2026
Ver todos los artículos relacionados

Video Experimental Relacionado

Updated: Sep 13, 2025

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
09:25

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

Published on: November 1, 2024

2.1K

Difusión de los aglutinantes de proteínas a las proteínas intrínsecamente desordenadas

Caixuan Liu1,2, Kejia Wu3,4,5, Hojun Choi1,2

  • 1Department of Biochemistry, University of Washington, Seattle, WA, USA.

Nature
|July 31, 2025
PubMed
Resumen
Este resumen es generado por máquina.

Los investigadores desarrollaron un nuevo método que utiliza la difusión de RF para generar enlaces proteicos de alta afinidad para proteínas intrínsecamente desordenadas (IDP) y regiones (IDR). Estos aglutinantes muestran potencial terapéutico, apuntando con éxito a las PDI y las RDI en modelos celulares y de enfermedades.

Más Videos Relacionados

Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain
14:25

Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain

Published on: December 12, 2017

18.2K
Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
07:24

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

1.9K

Videos de Experimentos Relacionados

Last Updated: Sep 13, 2025

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
09:25

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

Published on: November 1, 2024

2.1K
Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain
14:25

Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain

Published on: December 12, 2017

18.2K
Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
07:24

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

1.9K

Área de la Ciencia:

  • Biología estructural
  • Ingeniería de proteínas
  • Biotecnología

Sus antecedentes:

  • Las proteínas intrínsecamente desordenadas (IDP) y las regiones (IDR) carecen de estructuras estables, lo que plantea desafíos para las aplicaciones terapéuticas y de diagnóstico.
  • El desarrollo de enlaces específicos y de alta afinidad para estos objetivos flexibles es crucial, pero carece de una metodología general.

Objetivo del estudio:

  • Establecer un enfoque computacional general para el diseño de aglutinantes de proteínas dirigidos a proteínas intrínsecamente desordenadas (IDP) y regiones intrínsecamente desordenadas (IDR).
  • Demostrar el potencial terapéutico y diagnóstico de los aglutinantes generados frente a PID e IDR específicos.

Principales métodos:

  • Utilizó la difusión por radiofrecuencia, un método de diseño computacional de proteínas, para generar aglutinantes mediante el muestreo libre de las conformaciones de proteínas objetivo y de unión.
  • Se generan aglutinantes para las IDP (amilina, péptido C, VP48, BRCA1_ARATH) y las IDR (G3BP1, IL-2RG, proteína priónica) con conformaciones específicas.
  • Eficacia del aglutinante validada mediante mediciones de la constante de disociación in vitro (Kd) y imágenes de fluorescencia en las células.

Principales resultados:

  • Se generaron con éxito enlaces de alta afinidad (Kd: 3100 nM) para varios IDP e IDR, dirigidos a diversas conformaciones.
  • Se ha demostrado la unión celular de los aglutinantes generados a sus respectivos objetivos.
  • Aplicaciones funcionales exhibidas: el aglutinante G3BP1 interrumpió los gránulos de estrés, y el aglutinante de amilina inhibió la formación de amiloide y mejoró la detección.

Conclusiones:

  • El enfoque basado en la difusión de RF proporciona una metodología general para el diseño de enlaces a los IDP y IDR flexibles.
  • Los aglutinantes generados exhiben una alta afinidad, especificidad y actividad funcional en contextos celulares.
  • Este método es muy prometedor para el desarrollo de nuevas terapias y diagnósticos para enfermedades que involucran a PDI/PDI.