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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

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.
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Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...

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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.
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Related Experiment Video

Updated: Dec 9, 2025

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Published on: February 6, 2020

Controlled nanoparticleassembly through protein conformational changes.

Halil Bayraktar¹, Sudhanshu Srivastava¹, Chang-Cheng You¹

¹Department of Chemistry, University of Massachusetts, 710 North Pleasant Street, Amherst, Massachusetts 01003, USA. rotello@chem.umass.edu mknapp@chem.umass.edu.

|September 10, 2020

Summary

This summary is machine-generated.

Researchers explored how proteins like cytochrome c (Cyt c) and apo-cytochrome c (apo Cyt c) interact with gold nanoparticles (Au-TAsp) to build new nanomaterials. They found that the ratio of protein to nanoparticle controls assembly, enabling tunable material properties.

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Last Updated: Dec 9, 2025

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Area of Science:

Nanomaterials Science
Biomolecular Engineering
Protein-Nanoparticle Interactions

Background:

Proteins mediate programmed bottom-up assembly of synthetic nanomaterials.
Understanding protein-nanoparticle interactions is key for designing functional hybrid materials.

Purpose of the Study:

To investigate the controlled self-assembly of functionalized gold nanoparticles (Au-TAsp) with cytochrome c (Cyt c) and apo-cytochrome c (apo Cyt c).
To explore the role of electrostatic interactions and protein structure in nanomaterial formation.

Main Methods:

Utilized functionalized gold nanoparticles (Au-TAsp) and varying ratios of native Cyt c and unfolded apo Cyt c.
Analyzed self-assembly through complementary electrostatic interactions.
Investigated pH-dependent dispersibility and proteolytic cleavage for disassembly.

Main Results:

Au-TAsp formed discrete, water-soluble adducts with native Cyt c.
Unfolded apo Cyt c induced nanocomposite formation, with structure dependent on Cyt c:Au-TAsp ratio.
Soluble nanocomposites showed induced α-helix formation at low apo Cyt c ratios, while insoluble aggregates formed at high ratios.
Assembly was pH-dependent and reversible; aggregates were disassembled via proteolytic cleavage.

Conclusions:

Protein-nanoparticle ratio critically dictates the local structure and dispersibility of hybrid nanomaterials.
Demonstrated selective remodeling of these hybrid materials through controlled disassembly.
Highlights potential for programmed bottom-up assembly of functional nanomaterials.