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-protein Interfaces02:04

Protein-protein Interfaces

15.0K
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...
15.0K
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

4.6K
4.6K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

3.1K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
3.1K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.2K
2.2K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

9.9K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
9.9K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

2.1K
2.1K

También podría leer

Artículos Relacionados

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

Ordenar por
Same author

Kinetic and Structural Analysis of Two Linkers in the Tautomerase Superfamily: Analysis and Implications.

Biochemistry·2021
Same author

Parallel molecular mechanisms for enzyme temperature adaptation.

Science (New York, N.Y.)·2021
Same author

Human SIRT1 Multispecificity Is Modulated by Active-Site Vicinity Substitutions during Natural Evolution.

Molecular biology and evolution·2020
Same author

A strategy for large-scale comparison of evolutionary- and reaction-based classifications of enzyme function.

Database : the journal of biological databases and curation·2020
Same author

Structural Basis for the Asymmetry of a 4-Oxalocrotonate Tautomerase Trimer.

Biochemistry·2020
Same author

The CAFA challenge reports improved protein function prediction and new functional annotations for hundreds of genes through experimental screens.

Genome biology·2019

Video Experimental Relacionado

Updated: Mar 31, 2026

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
06:50

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

2.7K

Reprogramación evolutiva de la especificidad de la interacción proteína-proteína

Eyal Akiva1, Patricia C Babbitt2

  • 1Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco, San Francisco, CA 94158, USA.

Cell
|October 27, 2015
PubMed
Resumen

Los investigadores estudiaron la evolución de la interacción proteína-proteína utilizando un modelo de toxina-antitoxina. Encontraron que las proteínas intermedias y promiscuas probablemente facilitan las trayectorias evolutivas, evitando los estados no interactivos.

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

7.8K
In Vitro Directed Evolution of a Restriction Endonuclease with More Stringent Specificity
09:16

In Vitro Directed Evolution of a Restriction Endonuclease with More Stringent Specificity

Published on: March 25, 2020

7.9K

Videos de Experimentos Relacionados

Last Updated: Mar 31, 2026

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
06:50

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

2.7K
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

7.8K
In Vitro Directed Evolution of a Restriction Endonuclease with More Stringent Specificity
09:16

In Vitro Directed Evolution of a Restriction Endonuclease with More Stringent Specificity

Published on: March 25, 2020

7.9K

Área de la Ciencia:

  • Biología evolutiva
  • Biología molecular
  • La bioquímica

Sus antecedentes:

  • Las interacciones proteína-proteína (IPP) son cruciales para las funciones celulares.
  • La comprensión de las vías evolutivas de los IPP es esencial para comprender la complejidad biológica.

Objetivo del estudio:

  • Investigar las trayectorias evolutivas de las interacciones proteína-proteína.
  • Identificar los mecanismos potenciales que facilitan la evolución de IPP nuevos o modificados.

Principales métodos:

  • Construcción y secuenciación profunda de las bibliotecas de mutación.
  • Utilización de un sistema de toxina-antitoxina como modelo para el estudio de la evolución de los IPP.

Principales resultados:

  • Se han identificado vías evolutivas probables para los IPP.
  • La evidencia sugiere que las proteínas intermedias promiscuas facilitan las transiciones entre los estados de interacción.
  • Evitación observada de estados no interactivos durante la evolución.

Conclusiones:

  • La evolución de las interacciones proteína-proteína puede seguir principios generales aplicables en varios sistemas biológicos.
  • Los intermediarios promiscuos juegan un papel importante en la mediación de las transiciones evolutivas.
  • Los hallazgos contribuyen a comprender la evolución de las enzimas y los principios más amplios de la evolución de la interacción biológica.