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

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
Protein Organization01:13

Protein Organization

Overview
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.

También podría leer

Artículos Relacionados

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

Ordenar por
Same author

Chiral supramolecular alloys: programmable 2D-3D control <i>via</i> Co-assembly of isomorphous β-peptide foldamers.

Chemical communications (Cambridge, England)·2026
Same author

Refined Shockley-Queisser Framework-Guided Acceptor Design Enables Loss-Aware Bandgap Targeting in Organic Solar Cells.

Journal of the American Chemical Society·2026
Same author

Fusion Arrest and Triggered Release of Contents in Coacervates via Oxidation-Assisted Interfacial Coating.

Chembiochem : a European journal of chemical biology·2026
Same author

SIGMA: Shear-induced gelation by microbead aggregation in tubular flow systems.

Materials today. Bio·2026
Same author

Two-dimensional Pd-C bonded organometallic framework with dynamic packing transformations.

Chemical science·2026
Same author

Controlled high-yield assembly of gold nanoparticles <i>via</i> amide bond formation.

Chemical science·2026

Video Experimental Relacionado

Updated: May 28, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Arquitectura de péptido autoensamblado con forma de diente: plegado en forma.

Sunbum Kwon1, Hye Sun Shin, Jintaek Gong

  • 1Molecular-Level Interface Research Center, Department of Chemistry, KAIST, Daejeon 305-701, Korea.

Journal of the American Chemical Society
|October 12, 2011
PubMed
Resumen

Los investigadores demuestran el autoensamblaje molecular 3D controlado utilizando un plegador helicoidal de péptido β. Este fragmento de proteína artificial forma una estructura única en forma de diente molar en solución acuosa, imitando las arquitecturas naturales del colágeno.

Más Videos Relacionados

Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets
13:42

Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets

Published on: November 2, 2011

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides
09:54

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides

Published on: August 20, 2018

Videos de Experimentos Relacionados

Last Updated: May 28, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets
13:42

Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets

Published on: November 2, 2011

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides
09:54

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides

Published on: August 20, 2018

Área de la Ciencia:

  • La bioquímica es la bioquímica.
  • Ciencia de los materiales Ciencia de los materiales.
  • Nanotecnología La nanotecnología es la nanotecnología.

Sus antecedentes:

  • El autoensamblaje molecular es crucial para crear sistemas funcionales.
  • El autoensamblaje 2D está bien estudiado, pero el autoensamblaje molecular 3D sigue siendo un desafío.
  • Los fragmentos de proteínas artificiales (foldamers) ofrecen potencial para el autoensamblaje controlado.

Objetivo del estudio:

  • Para investigar el autoensamblaje en 3D de un plegador helicoidal de péptido β.
  • Para crear nuevas arquitecturas moleculares 3D.
  • Para comprender la disposición molecular en la estructura autoensamblada.

Principales métodos:

  • Síntesis de un plegador de péptido β helicoidal con estructura secundaria definida.
  • Inducir el autoensamblaje en solución acuosa.
  • Análisis por difracción de rayos X en polvo (PXRD). análisis.
  • Optimización global y refinamiento de Rietveld para la determinación estructural.

Principales resultados:

  • El plegador de péptido β se autoensambló en una arquitectura molecular 3D sin precedentes.
  • La estructura exhibió una forma distinta de diente molar.
  • PXRD y los métodos computacionales aclararon el arreglo molecular.
  • Cuatro monómeros helicoidales de mano izquierda formaron una superhélice de mano derecha dentro de la célula unitaria.

Conclusiones:

  • Los foldameres helicoidales de β-péptido pueden formar estructuras moleculares 3D complejas de forma controlada.
  • La estructura autoensamblada se asemeja a la arquitectura superenrollada del colágeno.
  • Este trabajo avanza en el campo del autoensamblaje molecular 3D y los materiales biomiméticos.