Video Experimental Relacionado
Updated: Jul 14, 2026
11:36
In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
Published on: July 25, 2019
Transferencia de elementos estructurales de estados compactos a estados extendidos en ubiquitina no disuelta
Stormy L Koeniger1, Samuel I Merenbloom, Sundarapandian Sevugarajan
1Department of Chemistry, Indiana University, Bloomington, Indiana 47405, USA.
Journal of the American Chemical Society
|August 31, 2006
Resumen
La espectrometría multidimensional de movilidad iónica (IMS, por sus siglas en inglés) revela cómo los iones de ubiquitina pasan de una estructura a otra en la fase gaseosa. Los hallazgos muestran que las estructuras compactas iniciales influyen en las formas alargadas finales, lo que indica una memoria estructural preservada durante el despliegue.
Área de la Ciencia:
- Química Física es la química física.
- Química biofísica y bioquímica.
- Biología Estructural Biología Estructural
Sus antecedentes:
- Las proteínas sufren cambios conformacionales cruciales para su función.
- El estudio de la estructura de la proteína en la fase gaseosa proporciona información sobre las propiedades intrínsecas.
- La espectrometría de movilidad iónica junto con la espectrometría de masas (IMS-MS) es una poderosa herramienta para el análisis estructural.
Objetivo del estudio:
- Para investigar las transiciones estructurales de los iones de ubiquitina en la fase gaseosa.
- Para entender cómo las conformaciones compactas iniciales influyen en la trayectoria de despliegue.
- Para determinar si la memoria estructural se retiene durante el despliegue de iones en fase gaseosa.
Principales métodos:
- Espectrometría multidimensional de movilidad iónica (IMS-IMS y IMS-IMS-IMS).
- Espectrometría de masas. espectrometría de masas.
- Activación selectiva de iones y análisis de las distribuciones estructurales.
Principales resultados:
- Se identificaron distintos conformadores de iones de ubiquitina compactos, parcialmente plegados y alargados.
- El despliegue de estados compactos produjo un espectro de intermedios parcialmente plegados y tres formas alargadas distintas.
- La distribución final de los conformes alargados dependía del estado compacto inicial, lo que sugiere una memoria estructural.
Conclusiones:
- Los iones de ubiquitina retienen la memoria de sus estructuras compactas iniciales durante el desarrollo de la fase gaseosa.
- Los intermediarios parcialmente plegados pueden transmitir información estructural a los estados finales.
- Los elementos de la estructura secundaria probablemente juegan un papel en la preservación de la memoria estructural a lo largo de la trayectoria de despliegue.
Videos de Conceptos Relacionados
01:57Protein Complexes with Interchangeable Parts
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 to...
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 to...
02:18The Proteasome
Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
01:38Intralumenal Vesicles and Multivesicular Bodies
Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...
01:57Protein Complexes with Interchangeable Parts
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 to...
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 to...
01:13The Proteasome
Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...
01:17The Proteasome Structure
The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
The proteasome is an...