Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

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 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...

Single-Strand DNA Binding Proteins

Single-Strand DNA Binding Proteins

For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...

Protein Organization

Protein Organization

Assembly of Cytoskeletal Filaments

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...

Molecular Chaperones and Protein Folding

Molecular Chaperones and Protein Folding

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...

You might also read

Related Articles

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

Sort by

Same journal

Bismuth Chalcogenide-Based Photocatalysts for Nitrogen Reduction: Recent Progress and Prospects.

Chemistry (Weinheim an der Bergstrasse, Germany)·2026

Same journal

A Cytosine‑Bulged (3+1) Hybrid G‑Quadruplex Formed by the Chicken DNA Replication Origin.

Chemistry (Weinheim an der Bergstrasse, Germany)·2026

Same journal

Mechanistic Insights Into Sustainable Catalytic Pyrolysis of Biomass-Derived Ferulic Acid: The Role of Alumina Regeneration.

Chemistry (Weinheim an der Bergstrasse, Germany)·2026

Same journal

Ru Nanoparticle Supported by Mesoporous SiO<sub>x</sub> and Pillared Montmorillonite: Suppressing Catalyst Inhibition in Carbon Dioxide Hydrogenation.

Chemistry (Weinheim an der Bergstrasse, Germany)·2026

Same journal

Hybrid Macrocyclic Peptides - Synthetic Strategies to Diversify and Cyclize Peptide Libraries in Phage Display Selections.

Chemistry (Weinheim an der Bergstrasse, Germany)·2026

Same journal

Interfacial Active Sites in Catalysts for Higher Alcohol Synthesis From CO<sub>2</sub>: A Review.

Chemistry (Weinheim an der Bergstrasse, Germany)·2026

Search research articles

Related Experiment Video

Updated: Jun 10, 2025

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

From Double-Stranded Helicates to Abiotic Double Helical Supramolecular Assemblies.

Victor Koehler¹

¹Adionics, The Advanced Ionic Solution, 17 bis avenue des Andes, 91940, Les Ulis, France.

Chemistry (Weinheim an Der Bergstrasse, Germany)

|October 21, 2024

Summary

Chemists create artificial double helices by mimicking nature's folding of oligomeric strands. These synthetic structures offer controlled self-assembly and potential for molecular recognition applications.

Keywords:

Double helix Foldamers Hybridization Self-assembly Supramolecular chemistry

More Related Videos

Self-assembling Morphologies Obtained from Helical Polycarbodiimide Copolymers and Their Triazole Derivatives

Self-assembling Morphologies Obtained from Helical Polycarbodiimide Copolymers and Their Triazole Derivatives

Published on: February 7, 2017

Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles

Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles

Published on: May 8, 2015

Related Experiment Videos

Last Updated: Jun 10, 2025

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

Self-assembling Morphologies Obtained from Helical Polycarbodiimide Copolymers and Their Triazole Derivatives

Self-assembling Morphologies Obtained from Helical Polycarbodiimide Copolymers and Their Triazole Derivatives

Published on: February 7, 2017

Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles

Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles

Published on: May 8, 2015

Area of Science:

Supramolecular Chemistry
Bio-inspired Materials Science

Background:

Nature utilizes oligomeric strand folding for functional assemblies.
Mimicking biomacromolecules drives the synthesis of artificial folded structures.
Non-covalent interactions enable self-assembly into complex supramolecular architectures.

Purpose of the Study:

To synthesize and characterize artificial secondary, tertiary, and quaternary structures.
To explore the formation of bio-inspired double helices from synthetic oligomers.
To investigate stimuli-responsive control over single- and double-helix equilibria.

Main Methods:

Design and synthesis of novel oligomers and polymers with encoded chemical information.
Characterization of self-assembled supramolecular architectures.
Investigation of double helix formation and stability using various stimuli (e.g., solvent, temperature).

Main Results:

Successful synthesis of diverse abiotic folded structures.
Demonstration of spontaneous self-assembly into functional supramolecular architectures.
Reported formation of stable synthetic double helices with controllable equilibria.

Conclusions:

Synthetic double helices represent a promising area for bio-inspired chemistry.
These structures exhibit potential for molecular recognition and future applications.
Stimuli-responsive control over helical structures is achievable.