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Related Concept Videos

Protein Complex Assembly02:41

Protein Complex Assembly

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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...
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Spindle Assembly02:50

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Spindle assembly occurs through three, often coexisting, pathways – the centrosome-mediated pathway, the chromatin-mediated pathway, and the microtubule-mediated pathway – collectively contributing to form a robust spindle apparatus.
In most cells, centrosomes are the primary microtubule nucleation centers. In the centrosome-mediated pathway, the G2-prophase transition triggers centrosome maturation and increased microtubule nucleation. Progressive nucleation results in a...
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Oligosaccharide Assembly01:24

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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
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Assembly of Cytoskeletal Filaments01:18

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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...
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Genome Annotation and Assembly03:36

Genome Annotation and Assembly

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The genome refers to all of the genetic material in an organism. It can range from a few million base pairs in microbial cells to several billion base pairs in many eukaryotic organisms. Genome assembly refers to the process of taking the DNA sequencing data and putting it all back together in a correct order to create a close representation of the original genome. This is followed by the identification of functional elements on the newly assembled genome, a process called genome annotation.
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Related Experiment Video

Updated: Jan 24, 2026

Chemical Dimerization-Induced Protein Condensates on Telomeres
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Self-assembly of a dimer system.

Mobolaji Williams1

  • 1Department of Physics, Harvard University, Cambridge, Massachusetts 02138, USA.

Physical Review. E
|May 22, 2019
PubMed
Summary

Self-assembly into dimers is either search-limited or combinatorics-limited. Most biological systems are search-limited, where finding partners, not combinatorial complexity, dictates dimerization.

Area of Science:

  • Statistical physics
  • Biophysics
  • Systems biology

Background:

  • Self-assembly drives the formation of essential biological structures like membranes and capsids.
  • Understanding the fundamental principles of self-assembly is crucial for molecular biology and nanotechnology.

Purpose of the Study:

  • To investigate the statistical physics of self-assembly using a simplified model of dimer formation from monomers.
  • To analytically determine the conditions governing dimer formation and classify systems based on limiting factors.

Main Methods:

  • Framing microstate counting as a combinatorial problem to derive an exact partition function.
  • Analyzing equilibrium conditions to classify dimer systems as "search-limited" or "combinatorics-limited."
  • Estimating biophysical quantities for DNA and protein interactions to validate the model.

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Related Experiment Videos

Last Updated: Jan 24, 2026

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Isolating Free Carbenes, their Mixed Dimers and Organic Radicals
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Main Results:

  • Dimer systems are categorized into "search-limited" and "combinatorics-limited" types.
  • Biological systems studied (DNA dimerization, protein interactions) are predominantly "search-limited."
  • The key constraint for correct dimerization is the product of particle diversity and volume, not number density.

Conclusions:

  • The ability of monomers to find each other (search limitation) is a more significant factor in biological dimerization than combinatorial complexity.
  • This work provides analytical insights into the combinatorics of self-assembly, applicable to various biological systems.