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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Assembly of Cytoskeletal Filaments01:18

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Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
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Assembly of Signaling Complexes01:30

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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
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Assembly of Complex Microtubule Structures01:32

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Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
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Cytoskeletal Accessory Proteins01:13

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The cytoskeleton is an essential cell component that plays several structural and functional roles. However, the filaments that make up the cytoskeleton cannot function independently and depend on the accessory or ancillary proteins to effectively carry out their function. Accessory proteins associate with cytoskeletal filaments and their monomers, aiding filament formation and function. They also help in the cross-communication among cytoskeletal filaments. Cytoskeletal accessory proteins are...
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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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Updated: Aug 28, 2025

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
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Conjuntos de proteínas simétricas alucinantes

B I M Wicky1,2, L F Milles1,2, A Courbet1,2,3

  • 1Department of Biochemistry, University of Washington, Seattle, WA, USA.

Science (New York, N.Y.)
|September 15, 2022
PubMed
Resumen
Este resumen es generado por máquina.

El aprendizaje profundo ahora puede diseñar nuevas estructuras simétricas de proteínas, incluidos los anillos grandes. Estos diseños de proteínas generados son estructuralmente precisos y amplían las posibilidades de los biomateriales y las nanomáquinas.

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Área de la Ciencia:

  • La bioquímica
  • Biología estructural
  • Biología computacional

Sus antecedentes:

  • Los modelos generativos de aprendizaje profundo ofrecen nuevas vías para explorar el espacio de la estructura de las proteínas.
  • Los métodos actuales se limitan a las secuencias y estructuras naturales de proteínas.

Objetivo del estudio:

  • Para generar nuevos homo-oligómeros de proteínas simétricas usando alucinaciones de red profunda.
  • Explorar el potencial del aprendizaje profundo en el diseño de arquitecturas complejas de proteínas.

Principales métodos:

  • Se empleó la alucinación de red profunda para generar estructuras de proteínas.
  • Las especificaciones incluían el número de protómeros y la longitud del protómero.
  • Validación experimental mediante cristalografía de rayos X y microscopía criolectrónica.

Principales resultados:

  • Se cristalizaron siete homooligómeros de proteínas diseñados, mostrando una alta similitud estructural con los modelos computacionales (mediana RMSD: 0,6 Å).
  • Se determinaron tres estructuras de anillo gigante (diámetro de 10 nm) con hasta 1550 residuos y simetría C33 a través de cryo-EM.
  • Las estructuras generadas difieren significativamente de las estructuras de proteínas conocidas anteriormente.

Conclusiones:

  • El aprendizaje profundo permite la creación de estructuras de proteínas diversas y nuevas.
  • Este enfoque abre posibilidades para diseñar nanomáquinas y biomateriales complejos basados en proteínas.