Search research articles

ACERCA DE JoVE

Visión General Liderazgo Blog Centro de Ayuda JoVE

AUTORES

Proceso de Publicación Consejo Editorial Alcance y Políticas Revisión por Pares Preguntas Frecuentes Enviar

BIBLIOTECARIOS

Testimonios Suscripciones Acceso Recursos Consejo Asesor de Bibliotecas Preguntas Frecuentes

INVESTIGACIÓN

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archivo

EDUCACIÓN

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Centro de Recursos para Profesores Sitio de Profesores

Términos y Condiciones de Uso

Política de Privacidad

Videos de Conceptos Relacionados

Catalysis

Catalysis

The presence of a catalyst affects the rate of a chemical reaction. A catalyst is a substance that can increase the reaction rate without being consumed during the process. A basic comprehension of a catalysts’ role during chemical reactions can be understood from the concept of reaction mechanisms and energy diagrams.

Introduction to Mechanisms of Enzyme Catalysis

Introduction to Mechanisms of Enzyme Catalysis

For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes...

Intrinsically Disordered Proteins

Intrinsically Disordered Proteins

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...

Conservation of Protein Domains Over Different Proteins

Conservation of Protein Domains Over Different Proteins

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...

Amplifying Signals via Enzymatic Cascade

Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...

Protein-protein Interfaces

Protein-protein Interfaces

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...

También podría leer

Artículos Relacionados

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

Ordenar por

Same author

Formate Dehydrogenase: The Role of the AMP Cofactor Fragment in Stabilization of the Transition State for Enzyme-Catalyzed Hydride Transfer.

ACS omega·2026

Same author

Enzyme Architecture: Activation of Phosphite Dehydrogenase-Catalyzed Hydride Transfer by NAD<sup>+</sup> Cofactor Fragments.

Biochemistry·2025

Same author

The Role of Protein Side Chains in Enzyme-Activating Conformational Changes: Lessons from Studies on Variant Enzymes.

Chemical reviews·2025

Same author

Bill Jencks' Model for Lifetime Enforced Changes in Reaction Mechanism: A Legacy for Physical Organic Chemistry.

Chemphyschem : a European journal of chemical physics and physical chemistry·2025

Same author

Glycerol 3-Phosphate Dehydrogenase Catalyzed Hydride Transfer: Enzyme Activation by Cofactor Pieces.

Biochemistry·2024

Same author

Glycerol 3-Phosphate Dehydrogenase: Role of the Protein Conformational Change in Activation of a Readily Reversible Enzyme-Catalyzed Hydride Transfer Reaction.

Biochemistry·2024

Search research articles

Video Experimental Relacionado

Updated: Jan 30, 2026

Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions

Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions

Published on: April 4, 2014

La flexibilidad y rigidez de las proteínas permiten una catálisis enzimática eficiente

John P Richard¹

¹Department of Chemistry , SUNY, University at Buffalo , Buffalo , New York 14260-3000 , United States.

Journal of the American Chemical Society

|February 1, 2019

Resumen

Las enzimas aceleran las reacciones estabilizando los estados de transición. La energía de unión de ligandos convierte las enzimas flexibles en formas rígidas y activas, mejorando la eficiencia y la especificidad catalítica.

Más Videos Relacionados

Simple Polyacrylamide-based Multiwell Stiffness Assay for the Study of Stiffness-dependent Cell Responses

Simple Polyacrylamide-based Multiwell Stiffness Assay for the Study of Stiffness-dependent Cell Responses

Published on: March 25, 2015

Fast Enzymatic Processing of Proteins for MS Detection with a Flow-through Microreactor

Fast Enzymatic Processing of Proteins for MS Detection with a Flow-through Microreactor

Published on: April 6, 2016

Videos de Experimentos Relacionados

Last Updated: Jan 30, 2026

Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions

Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions

Published on: April 4, 2014

Simple Polyacrylamide-based Multiwell Stiffness Assay for the Study of Stiffness-dependent Cell Responses

Simple Polyacrylamide-based Multiwell Stiffness Assay for the Study of Stiffness-dependent Cell Responses

Published on: March 25, 2015

Fast Enzymatic Processing of Proteins for MS Detection with a Flow-through Microreactor

Fast Enzymatic Processing of Proteins for MS Detection with a Flow-through Microreactor

Published on: April 6, 2016

Área de la Ciencia:

La bioquímica
Cinética de las enzimas
Dinámica de las proteínas

Sus antecedentes:

La catálisis enzimática se basa en la estabilización de las interacciones con los estados de transición de la reacción.
Las enzimas exhiben una mayor afinidad por los estados de transición que los sustratos, impulsando aceleraciones de velocidad.

Objetivo del estudio:

Investigar cómo la energía de unión de ligandos impulsa los cambios conformacionales de la enzima.
Generalizar los hallazgos sobre la flexibilidad y la actividad de las enzimas en diversas reacciones catalíticas.

Principales métodos:

Análisis experimental de la energía de unión de fosfodianiones en sustratos de monoésteres de fosfato.
Modelado computacional de cambios conformacionales impulsados por ligandos en la triosefosfato isomerasa.

Principales resultados:

La energía de unión al sustrato convierte las enzimas flexibles en complejos de Michaelis rígidos y activos.
La complejidad conformacional de la enzima se correlaciona con el aumento de la aceleración de la tasa.
Las estructuras enzimáticas flexibles, como los pliegues de barril TIM, evolucionan para utilizar la energía de unión para los cambios conformacionales.

Conclusiones:

La energía de unión de ligandos es crucial para moldear enzimas flexibles en estados catalíticamente activos.
Este mecanismo optimiza la expresión de las energías de unión del estado de transición, mejorando la especificidad de la enzima.
La dinámica de las proteínas juega un papel importante en la cinética y la evolución de las enzimas.