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Videos de Conceptos Relacionados

Formation of Intermediate Filaments00:57

Formation of Intermediate Filaments

Intermediate filaments are cytoskeletal proteins with higher tensile strength and flexibility than microfilaments and microtubules. Unlike the other two cytoskeletal proteins, intermediate filament formation lacks the enzymatic activity to hydrolyze nucleotides like ATP and GTP to generate energy for polymerization. Therefore, the formation of intermediate filaments is multistep self-assembly. The involvement of any accessory proteins in intermediate filament formation has not yet been reported.
Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
The Structure of Intermediate Filaments01:19

The Structure of Intermediate Filaments

The intermediate filaments are one of three widely studied cytoskeletal filaments. They are so named as their diameter (10 nm) is in between that of microfilaments (7 nm) and the microtubules (25 nm).  These filaments are highly stable and can remain intact when exposed to high salt concentrations and detergents. These filaments are responsible for providing stability and mechanical support to the cells. They also help in cell adhesion and maintaining tissue integrity.
Intermediate filaments...
Actin Polymerization01:42

Actin Polymerization

Actin polymerization occurs through the head-to-tail association of binding sites on monomeric actin or G-actin to form filamentous or F-actin. The polymerization can be divided into three phases ̶  nucleation, elongation, and steady-state phase.
The nucleation phase involves forming a stable nucleus consisting of three actin monomers to form a new actin filament. Actin-binding proteins such as formins and Arp2/3 complex help filament growth post-nucleation. The Formins form straight actin...
Types of Intermediate Filaments01:31

Types of Intermediate Filaments

The intermediate filaments are an essential component of the cytoskeleton. Presently six types of intermediate filament have been identified. Type I and II are acidic and basic keratin proteins. Type III is of mesodermal origin and comprises four proteins: vimentin, desmin, glial fibrillary acidic protein (GFAP), and peripherin. Vimentin is commonly found in mesenchymal cells, desmin in muscle cells, GFAP in astrocytes, while peripherin is found in peripheral nervous system neurons (PNS). Type...
Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...

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DNA Nanotubes as a Versatile Tool to Study Semiflexible Polymers
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Las fases de los nanofilamentos helicoidales en helical.

L E Hough1, H T Jung, D Krüerke

  • 1Department of Physics and Liquid Crystal Materials Research Center, University of Colorado, Boulder, CO 80309, USA. hough@colorado.edu

Science (New York, N.Y.)
|July 25, 2009
PubMed
Resumen
Este resumen es generado por máquina.

Las moléculas aquirales se autoensamblan en capas retorcidas y homoquirales dentro de filamentos a nanoescala. Esta estructura única forma una fase de cristal líquido con coherencia macroscópica, revelando un nuevo orden quiral.

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Área de la Ciencia:

  • Ciencia de los materiales Ciencia de los materiales.
  • La cristalografía es una técnica de cristalografía.
  • Física de la materia blanda Física de la materia blanda

Sus antecedentes:

  • La formación de cristales quirales típicamente implica quiralidad molecular, pero la torsión a menudo se expulsa de las celosías debido a la tensión.
  • Las moléculas achirales generalmente forman estructuras achirales, que carecen de mano inherente.

Objetivo del estudio:

  • Para investigar el estado ordenado de un material formado a partir de moléculas achirales que exhiben propiedades quirales.
  • Comprender cómo el confinamiento espacial influye en el ordenamiento molecular y la ruptura de simetría.

Principales métodos:

  • El autoensamblaje de moléculas aquirales en filamentos a nanoescala.
  • Análisis estructural de la organización en capas dentro de los filamentos.
  • Caracterización de la fase de cristal líquido macroscópico.

Principales resultados:

  • Las moléculas achirales se autoensamblan en filamentos de nanoescala ordenados periódicamente.
  • Las capas dentro de estos filamentos exhibieron una torsión significativa y una homoquiral rigurosa, una forma de simetría rota.
  • La organización colectiva de los filamentos condujo a una coherencia macroscópica de torsión, formando una fase de cristal líquido.

Conclusiones:

  • El confinamiento espacial en filamentos permite a las moléculas achirales formar estructuras quirales.
  • Este proceso de autoensamblaje supera la incompatibilidad de torsión con el ordenamiento en celosía.
  • La fase de cristal líquido resultante demuestra un nuevo mecanismo para la organización quiral macroscópica.