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 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...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
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...
Characteristics and Nomenclature of Copolymers01:24

Characteristics and Nomenclature of Copolymers

Copolymers are the products obtained from the polymerization of multiple monomer species. So, in a polymer chain itself, there can be multiple repeating units that come from different monomers. The process of synthesizing a polymer from different monomer species is called copolymerization. When two monomers are involved, the polymer is known as a bipolymer. Polymers with three and four monomers are termed terpolymers and quaterpolymers, respectively. Figure 1 depicts the copolymerization of...

You might also read

Related Articles

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

Sort by
Same author

Polymerized Short Sequences as a Template for Protein Folding and Evolution.

Nano letters·2026
Same author

Computational design of functional random heteropolymers through atomistic simulations.

PloS one·2026
Same author

Flow-Induced Microdomain Alignment During Block Copolymer Graphoepitaxy.

Advanced materials (Deerfield Beach, Fla.)·2026
Same author

Polyanion Chemistry Engineers Ternary RNA Nanoparticle Structure/Function from the Inside-Out.

ACS nano·2026
Same author

Random heteropolymers as enzyme mimics.

Nature·2025
Same author

Repetitive proteins that undergo large conformational changes evade structural prediction algorithms.

The Journal of chemical physics·2025
Same journal

Characterization of genomic diversity in bacteriophages infecting Rhodococcus.

PloS one·2026
Same journal

Effectiveness of the Responding to Experienced and Anticipated Discrimination (READ) training on reducing stigma for medical students in Tunisia.

PloS one·2026
Same journal

Cell-cell junction gene signatures as subtype-specific prognostic biomarkers in breast cancer.

PloS one·2026
Same journal

GC-MS based tentative identification of γ-sitosterol from Brassica nigra seeds and evaluation of its anticancer potential: An integrated in vitro and in silico study.

PloS one·2026
Same journal

Ad-based social media interventions increase belief accuracy and generate pro-social opinions among non-news readers.

PloS one·2026
Same journal

Negotiating knowledge: The role of network hedging in the production of high-impact science.

PloS one·2026
See all related articles

Related Experiment Video

Updated: May 31, 2026

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
10:17

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

Multimerization interactions between protein-inspired single-chain random heteropolymers.

Shayna L Hilburg1, Tianyi Jin1,2, Priya Ganesh1

  • 1Department of Materials Science and Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts, United States of America.

Plos One
|May 28, 2026
PubMed
Summary
This summary is machine-generated.

Single-chain nanoparticles (SCNPs) mimic proteins by forming multimers through side-chain interactions. Their conformation significantly influences multimerization, not sequence variation.

More Related Videos

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
08:34

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

Published on: February 5, 2020

Using Polystyrene-block-poly(acrylic acid)-coated Metal Nanoparticles as Monomers for Their Homo- and Co-polymerization
09:02

Using Polystyrene-block-poly(acrylic acid)-coated Metal Nanoparticles as Monomers for Their Homo- and Co-polymerization

Published on: July 9, 2015

Related Experiment Videos

Last Updated: May 31, 2026

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
10:17

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
08:34

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

Published on: February 5, 2020

Using Polystyrene-block-poly(acrylic acid)-coated Metal Nanoparticles as Monomers for Their Homo- and Co-polymerization
09:02

Using Polystyrene-block-poly(acrylic acid)-coated Metal Nanoparticles as Monomers for Their Homo- and Co-polymerization

Published on: July 9, 2015

Area of Science:

  • Polymer Chemistry
  • Biomaterials Science
  • Computational Chemistry

Background:

  • Single-chain nanoparticles (SCNPs) exhibit protein-like behaviors, making them promising for various applications.
  • Understanding SC NP interactions with other macromolecules is crucial for designing advanced materials.

Purpose of the Study:

  • To investigate the interaction mechanisms of SC Nps with other macromolecules using molecular dynamics simulations.
  • To characterize the multimerization behavior of methacrylate-based SC Nps in aqueous solutions.

Main Methods:

  • Molecular dynamics simulations were employed to model SC NP behavior.
  • Analysis focused on non-covalent assembly driven by hydrophobic effects and Flory-Huggins parameters.
  • Interaction modes and monomer enrichment at contact points were examined.

Main Results:

  • SC Nps demonstrated two main interaction modes: adsorption via side-chain interactions (similar to protein oligomerization) and maintenance of single-chain structures.
  • Amphiphilic monomers, particularly hydrophobic residues, enriched at contact interfaces during prolonged adsorption.
  • Polymer conformation played a significant role in multimerization, outweighing sequence variations.

Conclusions:

  • SC Nps can undergo multimerization through protein-like adsorption mechanisms.
  • The conformational dynamics of SC Nps are key determinants of their self-assembly and interaction behavior.
  • These findings provide insights into designing SC Nps for targeted macromolecular interactions.