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Related Concept Videos

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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Updated: Jun 21, 2026

DNA Nanotubes as a Versatile Tool to Study Semiflexible Polymers
08:00

DNA Nanotubes as a Versatile Tool to Study Semiflexible Polymers

Published on: October 25, 2017

Helical nanofilament phases.

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
Summary
This summary is machine-generated.

Achiral molecules self-assemble into twisted, homochiral layers within nanoscale filaments. This unique structure forms a liquid crystal phase with macroscopic coherence, revealing novel chiral ordering.

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Scalable Nanohelices for Predictive Studies and Enhanced 3D Visualization
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Drawing and Hydrophobicity-patterning Long Polydimethylsiloxane Silicone Filaments
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Drawing and Hydrophobicity-patterning Long Polydimethylsiloxane Silicone Filaments

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DNA Nanotubes as a Versatile Tool to Study Semiflexible Polymers
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Drawing and Hydrophobicity-patterning Long Polydimethylsiloxane Silicone Filaments
07:56

Drawing and Hydrophobicity-patterning Long Polydimethylsiloxane Silicone Filaments

Published on: January 7, 2019

Area of Science:

  • Materials Science
  • Crystallography
  • Soft Matter Physics

Background:

  • Chiral crystal formation typically involves molecular chirality, but twist is often expelled from lattices due to strain.
  • Achiral molecules usually form achiral structures, lacking inherent handedness.

Purpose of the Study:

  • To investigate the ordered state of a material formed from achiral molecules that exhibits chiral properties.
  • To understand how spatial confinement influences molecular ordering and symmetry breaking.

Main Methods:

  • Self-assembly of achiral molecules into nanoscale filaments.
  • Structural analysis of the layered organization within filaments.
  • Characterization of the macroscopic liquid crystal phase.

Main Results:

  • Achiral molecules self-assembled into periodically ordered nanoscale filaments.
  • Layers within these filaments exhibited significant twist and rigorous homochirality, a form of broken symmetry.
  • Collective organization of filaments led to macroscopic coherence of twist, forming a liquid crystal phase.

Conclusions:

  • Spatial confinement in filaments enables achiral molecules to form chiral structures.
  • This self-assembly process overcomes the incompatibility of twist with lattice ordering.
  • The resulting liquid crystal phase demonstrates a novel mechanism for macroscopic chiral organization.