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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...
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...
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.
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...
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: May 25, 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

Structure formation by dynamic self-assembly.

Liqiang Li1, Michael H Köpf, Svetlana V Gurevich

  • 1Physikalisches Institut, Universität Münster, Wilhelm-Klemm-Str. 10, Münster 48149, Germany.

Small (Weinheim an Der Bergstrasse, Germany)
|January 28, 2012
PubMed
Summary

This review covers a decade of research on creating nanoscale and microscale patterns on wafer-sized surfaces using dynamic self-assembly techniques like Langmuir-Blodgett (LB) transfer and dip-coating.

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Origami Inspired Self-assembly of Patterned and Reconfigurable Particles

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Area of Science:

  • Materials Science
  • Nanotechnology
  • Surface Chemistry

Background:

  • Fabrication of ordered nanoscale and microscale patterns is crucial for advanced materials and devices.
  • Controlling pattern dimensions and alignment over large areas presents significant challenges.
  • Dynamic self-assembly offers a promising route for scalable pattern fabrication.

Purpose of the Study:

  • To review advancements in mesostructured pattern fabrication over the last decade.
  • To present strategies for forming patterns from homogeneous Langmuir monolayers.
  • To explain the theoretical basis of pattern formation and summarize chemical patterning techniques.

Main Methods:

  • Langmuir-Blodgett (LB) transfer for pattern formation.
  • Dip-coating techniques for dynamic self-assembly.
  • Fabrication of mesostructured patterns with controlled shape, size, and alignment.

Main Results:

  • Successful fabrication of mesostructured patterns with lateral dimensions in the nano- and microscales.
  • Demonstrated control over pattern shape, size, and alignment using LB transfer.
  • Summarized patterning of nanocrystals and other chemicals via LB transfer and dip-coating.

Conclusions:

  • Dynamic self-assembly, particularly LB transfer and dip-coating, is effective for wafer-scale mesostructure fabrication.
  • Understanding the theoretical aspects of pattern formation is key to precise control.
  • These methods enable versatile patterning of various materials at the nanoscale.