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Related Concept Videos

Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

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...
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...
Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin networks...
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.
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
Introduction to Structures01:30

Introduction to Structures

A structure is defined as a system of interconnected members designed to support or transfer forces and successfully withstand the loads acting on them. The internal forces of a structure can be determined by decomposing the structure and analyzing the free-body diagrams of the individual members or of a combination of members. This helps in understanding the structural elements' behavior and ensuring that the structure is stable and can withstand the subjected loads.
There are three main...

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Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles
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Published on: May 8, 2015

Structural forces from directed self-assembly.

Panagiotis Angelikopoulos1, Saud Al Harthy, Henry Bock

  • 1Department of Chemical Engineering, Heriot-Watt University, Edinburgh, EH14 4AS, Scotland, UK.

The Journal of Physical Chemistry. B
|October 16, 2009
PubMed
Summary

Surfactants self-assemble around crossing carbon nanotubes, forming a micelle-like structure that generates forces between the tubes. This self-assembly offers a pathway for designing novel nanocomposite materials.

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Area of Science:

  • Materials Science
  • Nanotechnology
  • Physical Chemistry

Background:

  • Bottom-up design of nanocomposite materials is crucial for advanced applications.
  • Understanding self-assembly mechanisms at the nanoscale is key to controlling material properties.

Purpose of the Study:

  • To investigate a novel micelle-like aggregate formed by surfactants at the interface of crossing carbon nanotubes.
  • To characterize the forces generated by this aggregate and their dependence on inter-tube distance.

Main Methods:

  • Computational modeling and simulation of surfactant behavior around carbon nanotubes.
  • Analysis of aggregate formation criteria based on nanotube gap and micelle core diameter.
  • Characterization of the effective forces between nanotubes mediated by the surfactant aggregate.

Main Results:

  • Surfactant self-assembly into a micelle-like structure occurs when the gap between crossing carbon nanotubes is less than the bulk micelle core diameter.
  • The surfactant aggregate generates an effective force between the nanotubes.
  • This force exhibits complex distance dependence, including layering effects and significant attraction at larger distances.

Conclusions:

  • The observed surfactant self-assembly provides a viable candidate structure for the bottom-up design of nanocomposite materials.
  • The entropic nature of the attractive force, arising from surfactant head group confinement, is a key factor in inter-tube interactions.
  • This study offers insights into controlling nanoscale interactions for material design.