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

Oligosaccharide Assembly

Oligosaccharide Assembly

Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...

Cooperative Allosteric Transitions

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...

Cooperative Allosteric Transitions

Cooperative Allosteric Transitions

Cooperative Allosteric Transitions

Cooperative Allosteric Transitions

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...

Protein Folding

Protein Folding

You might also read

Related Articles

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

Sort by

Same author

Stabilizing in-transition phases of superlattices through shape control of silver nanocrystals.

Science (New York, N.Y.)·2026

Same author

Exploring entropy landscapes using hard particle Monte Carlo metadynamics.

Proceedings of the National Academy of Sciences of the United States of America·2026

Same author

Intermetallic nanoassemblies potentiate systemic STING activation.

Science (New York, N.Y.)·2026

Same author

Quantifying local point-group-symmetry order in complex particle systems.

The Journal of chemical physics·2026

Same author

Engineering low-symmetry colloidal crystals with optical anisotropies.

Science advances·2026

Same author

Using particle shape to control defects in colloidal crystals on spherical interfaces.

Soft matter·2026

Same journal

Nanopore sequencing with proteins: synchronization and dischronization of molecular dynamics simulations with laboratory and industrial developments.

Soft matter·2026

Same journal

Catanionics from biosurfactants and regular surfactants: miscibility and structure.

Soft matter·2026

Same journal

Adhesives with a thickness smaller than the fractocohesive length enhance adhesion.

Soft matter·2026

Same journal

Non-equilibrium phase transitions in hybrid Voronoi models of cell colonies.

Soft matter·2026

Same journal

Effects of methoxy substituents on self-assembly and gelation performance of benzamide-based organogelators.

Soft matter·2026

Same journal

Rheology of <i>Escherichia coli</i> suspensions with various bacterial morphologies and motion characteristics.

Soft matter·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Apr 7, 2026

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

Shape allophiles improve entropic assembly.

Eric S Harper¹, Ryan L Marson, Joshua A Anderson

¹Department of Materials Science and Engineering, University of Michigan, Ann Arbor, Michigan 48109, USA.

|July 7, 2015

Summary

This summary is machine-generated.

Shape allophiles, particles designed to fit like puzzle pieces, control entropic forces for self-assembly. This method enables the creation and stabilization of specific structures, like square lattices, from simple shapes.

More Related Videos

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

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

Published on: August 2, 2012

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

Related Experiment Videos

Last Updated: Apr 7, 2026

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

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

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

Published on: August 2, 2012

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

Area of Science:

Materials Science
Statistical Mechanics
Supramolecular Chemistry

Background:

Controlling self-assembly is crucial for creating ordered materials.
Entropic forces play a significant role in molecular self-organization.
Designing particles with specific interaction properties is key to directing assembly.

Purpose of the Study:

To introduce and investigate "shape allophiles" for controlled self-assembly.
To demonstrate the use of directional entropic forces in stabilizing desired structures.
To explore the application of allophilic shaping for lattice formation.

Main Methods:

Analyzing particle interactions using potential of mean force and torque.
Quantifying binding through the fraction of entropically bound particles.
Simulating and generalizing assembly behavior of shaped particles.

Main Results:

Demonstrated successful re-assembly of squares and self-assembly of a square lattice using allophilic shaping.
Showcased the ability to assemble triangles into a square lattice via allophilic design.
Validated the principle of controlling structure formation through designed particle shapes and interactions.

Conclusions:

Shape allophiles offer a novel strategy for directed self-assembly.
Allophilic design provides a method to stabilize desired material phases.
This approach has potential applications in materials science and nanotechnology.