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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...
Protein Complex Assembly02:41

Protein Complex Assembly

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.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Complex Assembly02:41

Protein Complex Assembly

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.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
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.
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...
Assembly of Complex Microtubule Structures01:32

Assembly of Complex Microtubule Structures

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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Related Experiment Video

Updated: Jun 10, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Protein assembly along a supramolecular wire.

Marion K Müller1, Katja Petkau, Luc Brunsveld

  • 1Chemical Genomics Centre of the Max Planck Society, Otto-Hahn Straße 15, 44227 Dortmund, Germany.

Chemical Communications (Cambridge, England)
|August 24, 2010
PubMed
Summary

Discotic molecules form self-assembled supramolecular wires. These wires serve as platforms for directed protein assembly using biotin functionalities.

Area of Science:

  • Supramolecular chemistry
  • Biotechnology
  • Materials science

Background:

  • Discotic molecules are known for their self-assembly properties.
  • Supramolecular structures offer unique platforms for molecular organization.
  • Biotinylation is a common strategy for biomolecular conjugation.

Purpose of the Study:

  • To investigate the self-assembly of discotic molecules into functional supramolecular wires.
  • To demonstrate the utility of these wires as platforms for directed protein assembly.
  • To explore the role of biotin functionalities in mediating protein attachment.

Main Methods:

  • Synthesis and characterization of discotic molecules.
  • Self-assembly studies to form supramolecular wires.

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Controlling the Size, Shape and Stability of Supramolecular Polymers in Water

Published on: August 2, 2012

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  • Protein binding assays utilizing biotin-streptavidin interactions.
  • Main Results:

    • Discotic molecules successfully self-assembled into ordered supramolecular wires.
    • The supramolecular wires effectively directed the assembly of proteins.
    • Biotin functionalities on the wires facilitated specific and stable protein attachment.

    Conclusions:

    • Discotic molecule-based supramolecular wires provide a versatile platform for protein assembly.
    • This approach enables controlled organization of proteins for potential applications in nanotechnology and biosensing.
    • The integration of biotinylation enhances the functionality of these supramolecular constructs.