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Related Concept Videos

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...
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.
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
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 Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

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Related Experiment Video

Updated: Jun 8, 2026

Origami Inspired Self-assembly of Patterned and Reconfigurable Particles
12:33

Origami Inspired Self-assembly of Patterned and Reconfigurable Particles

Published on: February 4, 2013

Self-assembly, modularity, and physical complexity.

S E Ahnert1, I G Johnston, T M A Fink

  • 1University of Cambridge, Cambridge CB3 0HE, UK.

Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics
|September 28, 2010
PubMed
Summary
This summary is machine-generated.

We developed a new method to quantify physical complexity based on self-assembly information. This approach reveals that biological structures favor symmetry and modularity, offering insights into molecular and protein complex organization.

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

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Last Updated: Jun 8, 2026

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

Published on: November 21, 2013

Area of Science:

  • Physics
  • Computational Biology
  • Information Theory

Background:

  • Quantifying physical complexity is challenging.
  • Self-assembly is a fundamental process in nature and nanotechnology.
  • Understanding structural complexity aids in designing novel materials and analyzing biological systems.

Purpose of the Study:

  • To introduce a novel quantitative measure of physical complexity.
  • To demonstrate the measure's applicability to diverse self-assembling structures.
  • To investigate the prevalence of symmetry and modularity in biological self-assembly.

Main Methods:

  • Developed an information-theoretic approach to quantify physical complexity.
  • Applied the measure to self-assembling polyominoes as a model system.
  • Extended the application to quantify complexity in molecules and protein complexes.

Main Results:

  • The proposed measure quantifies physical complexity based on self-assembly information requirements.
  • Demonstrated adaptability to various geometries and structures composed of building blocks.
  • Identified symmetry and modularity as key features favored in biological self-assembly, particularly in protein complexes.
  • Introduced joint, mutual, and conditional complexity for comparing physical structures.

Conclusions:

  • The new quantitative measure provides a robust framework for assessing physical complexity.
  • Symmetric and modular structures are evolutionarily favored in biological self-assembly.
  • The developed concepts of joint, mutual, and conditional complexity offer new tools for structural analysis.