Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

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...
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...
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...
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...
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,...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Signaling and Mechanistic Insights into Folate Binding Protein-Induced Cytotoxicity in KB Cancer Cells.

Molecular pharmaceutics·2025
Same author

Atomic Force Microscopy Infrared Spectroscopy Method for Multisample Comparison of Topographic, Infrared Imaging, and Stiffness Domains.

Analytical chemistry·2025
Same author

Bacterial species-structure-property relationships of polyhydroxyalkanoate biopolymers produced on simple sugars for thin film applications.

Microbial cell factories·2025
Same author

Impact of Heat and Acidic Stress on the Biochemical Composition of <i>Pseudomonas aeruginosa</i> Bacteriophages─A Nanoscale AFM-IR Study.

Analytical chemistry·2025
Same author

Viperin expression leads to downregulation of mitochondrial genes through misincorporation of ddhCTP by mitochondrial RNA polymerase.

The Journal of biological chemistry·2025
Same author

The role of N-terminal acetylation of COVID fusion peptides in the interactions with liquid-ordered lipid bilayers.

Journal of colloid and interface science·2024

Related Experiment Video

Updated: May 15, 2026

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
10:01

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

Evaluation of a symmetry-based strategy for assembling protein complexes.

Dustin P Patterson1, Ankur M Desai, Mark M Banaszak Holl

  • 1Department of Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.

RSC Advances
|January 8, 2013
PubMed
Summary

Scientists designed fusion proteins to self-assemble into cage-like structures. The strategy successfully created defined globular protein complexes, primarily dimers and tetramers, demonstrating controlled protein assembly.

More Related Videos

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
09:30

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

Published on: August 6, 2018

A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

Related Experiment Videos

Last Updated: May 15, 2026

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
10:01

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
09:30

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

Published on: August 6, 2018

A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Engineering

Background:

  • Protein self-assembly is crucial for biological function.
  • Designing artificial protein assemblies requires precise control over protein interactions.
  • Leveraging native protein symmetry can guide the formation of complex structures.

Purpose of the Study:

  • To evaluate a strategy for assembling proteins into defined cage-like structures.
  • To engineer fusion proteins capable of self-assembly based on quaternary structure symmetry.
  • To investigate the assembly behavior of designed fusion proteins using KDPG aldolase.

Main Methods:

  • Design of two fusion proteins (A-(+) and A-(-)) incorporating KDPG aldolase, a flexible spacer, and a coiled-coil interaction domain.
  • Incubation of A-(+) and A-(-) to induce self-assembly.
  • Characterization of assembled complexes using size exclusion chromatography coupled with multi-angle laser light scattering (SEC-MALS), analytical ultracentrifugation (AUC), transmission electron microscopy (TEM), and atomic force microscopy (AFM).

Main Results:

  • The designed fusion proteins self-assembled into a mixture of globular complexes upon incubation.
  • Analysis confirmed the predominant formation of dimeric and tetrameric complexes of A-(+) and A-(-).
  • Evidence for larger assemblies, such as octameric complexes, was also observed, indicating scalability of the strategy.

Conclusions:

  • The protein assembly strategy, based on native symmetry and engineered heterodimeric interactions, yields defined protein structures.
  • The inherent flexibility of the fusion protein design allows for the formation of a limited range of globular assemblies.
  • This approach provides a foundation for constructing larger, ordered protein nanomaterials.