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Protein Complex Assembly

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 Assembly

Protein Complex Assembly

Disassembly of Intermediate Filaments

Disassembly of Intermediate Filaments

Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...

Protein Folding

Protein Folding

Protein Folding

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...

Noncovalent Attractions in Biomolecules

Noncovalent Attractions in Biomolecules

Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...

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Related Experiment Video

Updated: Jan 13, 2026

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

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

Published on: November 21, 2013

The interplay between biomolecular assembly and phase separation.

Giacomo Bartolucci^1,2, Ivar S Haugerud², Thomas C T Michaels³

¹Max Planck Institute for the Physics of Complex Systems, Dresden, Germany.

|January 9, 2026

Summary

This summary is machine-generated.

This study introduces a thermodynamic theory explaining how molecular assembly and phase separation interact. The findings align with experimental data on protein condensates, offering insights into cellular functions and neurodegenerative diseases.

Keywords:

assembly kinetics biochemistry chemical biology molecular assembly none phase separation

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Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

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Published on: August 6, 2018

Area of Science:

Biophysics
Molecular Biology
Thermodynamics

Background:

Biological functions involve molecular assembly and biomolecular condensate formation.
Condensed phases typically form through phase separation.
Molecular assemblies are clusters of molecules with diverse characteristics.

Purpose of the Study:

To develop a thermodynamic theory for the interplay between molecular assembly and phase separation.
To understand the equilibrium states and relaxation dynamics of protein interactions.
To provide a framework for studying cellular and disease-associated assemblies.

Main Methods:

Developed a theory based on thermodynamic principles.
Proposed two prototypical classes of protein interactions.
Characterized equilibrium states and relaxation dynamics.

Main Results:

Obtained results consistent with in vitro experimental observations of reconstituted proteins.
Observed anomalous size distribution of assemblies.
Documented gelation of condensed phases and changes in condensate volume during aging.

Conclusions:

The developed theory offers a framework to understand physiological and aberrant molecular assemblies.
Insights gained are relevant to cellular function and neurodegenerative disorders.
The theory bridges molecular assembly, phase separation, and condensate behavior.