Jove
Visualize
Contáctanos

Videos de Conceptos Relacionados

Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

11.4K
Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
11.4K
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 Organization01:24

Protein Organization

7.3K
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....
7.3K
Conservation of Protein Domains02:26

Conservation of Protein Domains

3.2K
3.2K
Protein and Protein Structure02:15

Protein and Protein Structure

81.5K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
81.5K
Protein and Protein Structures02:15

Protein and Protein Structures

10.9K
10.9K

También podría leer

Artículos Relacionados

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

Ordenar por
Same author

Biomimetic ferroelectric-semiconductor transistor enables neuronal multisensory integration.

Nature communications·2026
Same author

Integrated Transcriptome Landscape of mRNAs, lncRNAs, circRNAs, and miRNAs Reveals Molecular Regulatory Networks of Sex Differentiation in the Zig-Zag Eel (<i>Mastacembelus armatus</i>).

International journal of molecular sciences·2026
Same author

Restoring BECN1-mediated autophagy mitigates acute lung injury caused by zinc oxide nanoparticles.

Free radical biology & medicine·2026
Same author

Multiplexed, precise genome engineering in monocots with twin prime editing systems.

Nature biotechnology·2026
Same author

Thioredoxin attenuates ischemia-reperfusion-induced pressure ulcer formation by enhancing HIF-1α/BNIP3-dependent mitophagy and suppressing MAPK/NF-κB signaling.

Archives of biochemistry and biophysics·2026
Same author

The effect and molecular mechanism of N-Acetylglucosamine transferase-V in the pathogenesis of cancers.

Glycobiology·2026
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

Video Experimental Relacionado

Updated: Sep 16, 2025

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins
05:08

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins

Published on: July 8, 2025

370

Avanzar en la evolución de las proteínas con modelos de plegamiento inverso que integran restricciones estructurales

Hongyuan Fei1, Yunjia Li2, Yijing Liu2

  • 1New Cornerstone Science Laboratory, Center for Genome Editing, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, China.

Cell
|July 8, 2025
PubMed
Resumen

Las restricciones informadas por IA para la ingeniería de proteínas (AiCE) mejoran la eficiencia de la evolución de las proteínas. Este método utiliza modelos de plegado inverso y restricciones para diseñar mutaciones de alta aptitud, superando las técnicas tradicionales.

Palabras clave:
El objetivo es:Optimización del editor baseAcoplamiento evolutivoEdición del genomamutaciones de alta aptitudplegado inversoEvolución de las proteínasrestricciones basadas en la estructura

Más Videos Relacionados

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

7.4K
Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
10:58

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Published on: July 25, 2013

17.2K

Videos de Experimentos Relacionados

Last Updated: Sep 16, 2025

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins
05:08

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins

Published on: July 8, 2025

370
Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

7.4K
Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
10:58

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Published on: July 25, 2013

17.2K

Área de la Ciencia:

  • Biotecnología
  • Biología computacional
  • Ingeniería de proteínas

Sus antecedentes:

  • Los métodos tradicionales de ingeniería de proteínas se enfrentan a desafíos con bajas tasas de éxito y altos costos.
  • Los enfoques actuales a menudo se basan en la experiencia humana y en modelos específicos de tareas, lo que limita la escalabilidad.

Objetivo del estudio:

  • Introducir restricciones informadas por IA para la ingeniería de proteínas (AiCE) para una evolución eficiente de proteínas artificiales.
  • Para demostrar la versatilidad y la superioridad de AiCE sobre los métodos convencionales de ingeniería de proteínas.

Principales métodos:

  • Utilizando modelos genéricos de plegado inverso de proteínas para muestrear secuencias.
  • Integrar las restricciones estructurales y evolutivas para identificar mutaciones de alta aptitud.
  • Aplicación de AiCE a diversas tareas de ingeniería de proteínas, incluidas las desaminasas, las secuencias de localización nuclear, las nucleasas y la transcriptasa inversa.

Principales resultados:

  • Las tasas de éxito alcanzadas oscilan entre el 11% y el 88% en ocho aplicaciones distintas de ingeniería de proteínas.
  • Se desarrollaron nuevos editores de bases: enABE8e (ventana de 5 bp), enSdd6-CBE (fidelidad mejorada de 1,3 veces) y enDdd1-DdCBE (actividad mitocondrial mejorada de hasta 14,3 veces).
  • Se ha demostrado la eficacia de AiCE en proteínas de diferentes tamaños, desde decenas hasta miles de residuos.

Conclusiones:

  • AiCE es un método de diseño de mutación versátil y fácil de usar.
  • AiCE mejora significativamente la eficiencia, la escalabilidad y la generalización en la ingeniería de proteínas.
  • Los editores de base desarrollados son prometedores para aplicaciones en medicina de precisión y agricultura.