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

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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...
Protein Folding01:25

Protein Folding

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...
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:22

Protein Folding

Overview
The Unfolded Protein Response01:37

The Unfolded Protein Response

The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...

También podría leer

Artículos Relacionados

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

Ordenar por
Same author

<i>De novo</i> design of transmembrane accessory subunits for fold stabilization and expansion.

bioRxiv : the preprint server for biology·2026
Same author

CRISPR-based functional analysis of chicken IRF9 reveals distinct modulation of dsRNA stimulated innate immune pathways.

Developmental and comparative immunology·2026
Same author

The lipid bilayer strengthens the cooperative network of membrane proteins.

Science advances·2025
Same author

Steric trapping strategy for studying the folding of helical membrane proteins.

Methods (San Diego, Calif.)·2024
Same author

Acute Decompensated Heart Failure in the Elderly: An Observational Study in a Regional Victorian Hospital.

Cureus·2024
Same author

Understanding the Clinical Profile and Hospitalisation Patterns of Residents From Aged Care Facilities: A Regional Victorian Hospital Study.

Cureus·2023

Video Experimental Relacionado

Updated: Jun 20, 2026

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
07:33

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Published on: October 15, 2018

Proteína desplegándose con una trampa estéril.

Tracy M Blois1, Heedeok Hong, Tae H Kim

  • 1Department of Chemistry and Biochemistry, UCLA-DOE Institute for Genomics and Proteomics, University of California, Los Angeles, California 90095, USA.

Journal of the American Chemical Society
|September 11, 2009
PubMed
Resumen

Este estudio introduce el atrapamiento estérico, un nuevo método para estudiar el plegamiento y la estabilidad de las proteínas en condiciones nativas. Esta técnica utiliza etiquetas de biotina y estreptavidina para impulsar y monitorear el despliegue de proteínas sin alterar las condiciones del disolvente.

Más Videos Relacionados

Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers
09:33

Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers

Published on: March 21, 2025

Nanomanipulation of Single RNA Molecules by Optical Tweezers
06:59

Nanomanipulation of Single RNA Molecules by Optical Tweezers

Published on: August 20, 2014

Videos de Experimentos Relacionados

Last Updated: Jun 20, 2026

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
07:33

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Published on: October 15, 2018

Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers
09:33

Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers

Published on: March 21, 2025

Nanomanipulation of Single RNA Molecules by Optical Tweezers
06:59

Nanomanipulation of Single RNA Molecules by Optical Tweezers

Published on: August 20, 2014

Área de la Ciencia:

  • La bioquímica es la bioquímica.
  • Biología Molecular Biología Molecular
  • Dinámica de las proteínas Dinámica de las proteínas.

Sus antecedentes:

  • El plegamiento de las proteínas es crucial para la función biológica.
  • Los métodos actuales para estudiar el despliegue de proteínas alteran las condiciones de la solución, afectando las fuerzas moleculares.
  • Se necesita un método para inducir y estudiar el despliegue en condiciones de disolvente nativo.

Objetivo del estudio:

  • Introducir un nuevo método, el atrapamiento estérico, para estudiar el plegamiento y la estabilidad de las proteínas.
  • Para permitir el despliegue y análisis de proteínas sin desestabilizar las condiciones del disolvente.
  • Investigar la dinámica de despliegue de proteínas y su estabilidad en ambientes fisiológicos.

Principales métodos:

  • El método de la trampa estérica consiste en etiquetar una proteína objetivo con dos etiquetas de biotina espacialmente cercanas.
  • La unión de la estreptavidina a ambas etiquetas depende del despliegue de la proteína.
  • El acoplamiento energético entre la unión de la estreptavidina y el despliegue de la proteína impulsa el proceso.

Principales resultados:

  • El método de la trampa estérica conduce con éxito el despliegue de la dihidrofolato reductasa (DHFR).
  • La aparente afinidad de unión a la streptavidina se correlaciona con cambios en la estabilidad del DHFR.
  • La DHFR se puede bloquear en un estado desplegado utilizando la tasa de desaceleración lenta de la estreptavidina.

Conclusiones:

  • El atrapamiento estérico ofrece un enfoque novedoso para estudiar el plegamiento de proteínas y la estabilidad en condiciones de disolvente nativo.
  • Este método permite el despliegue específico de los dominios proteicos seleccionados.
  • La técnica de la trampa estérica muestra una aplicación potencial a las proteínas de la membrana.