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

10.6K
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...
10.6K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

17.9K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
17.9K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

5.7K
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,...
5.7K
Protein Folding01:25

Protein Folding

7.9K
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...
7.9K

You might also read

Related Articles

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

Sort by
Same author

The Phosphate-Bridged Pentapalladium(II)-Containing 18-Tungsto-4-Phosphate [Pd<sub>5</sub>O<sub>2</sub>(HPO<sub>4</sub>)<sub>2</sub>(PW<sub>9</sub>O<sub>34</sub>)<sub>2</sub>]<sup>16-</sup>: Synthesis and Physicochemical Properties.

Inorganic chemistry·2026
Same author

Cation-Directed Host-Guest Assembly and Reversible Wheel to Cluster Interconversion in a 20-Molybdate System.

Chemistry (Weinheim an der Bergstrasse, Germany)·2026
Same author

Dynamic proteomics of Nasonia vitripennis pupal development reveals testis-specific regulation of new proteins (orphans) likely related to exo-α-sialidases.

BMC genomics·2026
Same author

Engineering β-cyclodextrin gels with nanoparticles: tunable assembly and multifunctional applications.

Nanoscale advances·2026
Same author

Inter cross-linking microgels by superchaotropic nano-ions at interface: Controlled stabilization of emulsions.

Journal of colloid and interface science·2025
Same author

Encapsulants Affect Liposome Surface Interactions with Biological Systems.

Small (Weinheim an der Bergstrasse, Germany)·2025
Same journal

Fundamentals, Measurement and Regulation of the Conductance of Single Molecule Junctions.

Angewandte Chemie (International ed. in English)·2026
Same journal

Quantitative Photoswitching of Spin States in o-Fluoroazobenzene-Loaded Metal-Organic Frameworks.

Angewandte Chemie (International ed. in English)·2026
Same journal

Cobalt Nanoparticles Confined in Defective Carbon Matrices for Robust Intermittent CO<sub>2</sub> Methanation.

Angewandte Chemie (International ed. in English)·2026
Same journal

Copper(II/III) Redox Couple Enables C─H Methylation via a Radical Mechanism Analogous to SAM Enzymes.

Angewandte Chemie (International ed. in English)·2026
Same journal

Ring Strain Engineering of Cyclic Ethers for High-Performance Sodium Metal Batteries.

Angewandte Chemie (International ed. in English)·2026
Same journal

Bond Length as a Unified Descriptor for Stable Iodine Battery.

Angewandte Chemie (International ed. in English)·2026
See all related articles

Related Experiment Video

Updated: Jun 18, 2025

Controlling the Size, Shape and Stability of Supramolecular Polymers in Water
16:24

Controlling the Size, Shape and Stability of Supramolecular Polymers in Water

Published on: August 2, 2012

18.6K

Controlling Protein Assembly with Superchaotropic Nano-Ions.

Ioanna Chazapi1, Tania Merhi1, Coralie Pasquier1

  • 1ICSM, Univ Montpellier, CEA, CNRS, ENSCM, Bagnols-sur-Cèze, 30207, France.

Angewandte Chemie (International Ed. in English)
|July 31, 2024
PubMed
Summary
This summary is machine-generated.

Super-chaotropic nano-ions, like boron clusters, reversibly assemble model proteins into 2D structures. These boron-based nano-ions act as a molecular glue, controlling assembly size and preserving protein structure.

Keywords:
boron clustersnano-ionsprotein assemblysuperchaotropic effect

More Related Videos

Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro
10:01

Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro

Published on: April 8, 2020

5.8K
Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution
11:55

Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution

Published on: August 16, 2016

11.7K

Related Experiment Videos

Last Updated: Jun 18, 2025

Controlling the Size, Shape and Stability of Supramolecular Polymers in Water
16:24

Controlling the Size, Shape and Stability of Supramolecular Polymers in Water

Published on: August 2, 2012

18.6K
Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro
10:01

Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro

Published on: April 8, 2020

5.8K
Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution
11:55

Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution

Published on: August 16, 2016

11.7K

Area of Science:

  • Biotechnology
  • Materials Science
  • Biochemistry

Background:

  • Protein assemblies are vital in biological systems but challenging to engineer.
  • Controlled assembly of proteins is a key goal in biotechnology.

Purpose of the Study:

  • To investigate the use of anionic boron clusters (super-chaotropic nano-ions) for inducing and controlling protein assembly.
  • To explore the effect of these nano-ions on protein structure and stability.

Main Methods:

  • Utilized anionic boron clusters, including COSAN- and halogenated closo-dodecarboranes (B12X12 2-), as nano-ions.
  • Induced 2D assembly formation of model proteins: myoglobin, carbonic anhydrase, and trypsin inhibitor.
  • Varied nano-ion concentration to control assembly size and assessed protein secondary structure.

Main Results:

  • Anionic boron clusters successfully induced the formation of 2D protein assemblies.
  • Nano-ion concentration reversibly controlled the size of the protein assemblies.
  • Protein secondary structures were minimally affected, and myoglobin's thermal denaturation was prevented.

Conclusions:

  • Inorganic boron-based nano-ions function as a reversible molecular glue for protein assembly.
  • This offers a novel approach for developing controlled protein assemblies.
  • The findings highlight potential applications in protein stabilization and engineering.