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

Hydrogen Bonds01:04

Hydrogen Bonds

A hydrogen bond is formed when a weakly positive hydrogen atom already bonded to one electronegative atom (for example, the oxygen in the water molecule) is attracted to another electronegative atom from another polar molecule, such as water (H2O), hydrogen fluoride (HF), or ammonia (NH3). The huge electronegativity difference between the H atom (2.1) and the atom to which it is bonded (4.0 for an F atom, 3.5 for an O atom, or 3.0 for an N atom), combined with the very small size of an H atom...
Hydrogen Bonds00:26

Hydrogen Bonds

Hydrogen BondsHydrogen bonds are weak attractions between atoms that have formed other chemical bonds. One of these atoms is electronegative, like oxygen, and has a partial negative charge. The other is a hydrogen atom that has bonded with another electronegative atom and has a partial positive charge.Hydrogen Bonds Control the World!Because hydrogen has very weak electronegativity when it binds with a strongly electronegative atom, such as oxygen or nitrogen, electrons in the bond are...
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:25

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 Organization01:13

Protein Organization

Overview
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.

You might also read

Related Articles

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

Sort by
Same author

Response to comment on "Serum ANGPTL4 as a biomarker for hemorrhagic transformation after endovascular therapy in acute ischemic stroke".

Journal of the Formosan Medical Association = Taiwan yi zhi·2026
Same author

Genetic Variants and Clinical Characteristics of Young-Onset Parkinson's Disease in the Hakka Population of Western Fujian.

Brain and behavior·2026
Same author

Serum angiopoietin-like protein 4 as a predictor of hemorrhagic transformation post-endovascular therapy in acute ischemic stroke: A prospective study.

Journal of the Formosan Medical Association = Taiwan yi zhi·2026
Same author

Endovascular Treatment of Medium-Vessel-Occlusion Strokes.

The New England journal of medicine·2026
Same author

Construction of a <sup>89</sup>Zr-Labeled Specific Antibody Fragment for the Noninvasive Detection of Mesothelin-Overexpressing Tumors.

Molecular pharmaceutics·2026
Same author

Divergent molecular mechanisms underlie differential toxicity of trivalent lanthanum and divalent cadmium in Enchytraeus crypticus.

Ecotoxicology and environmental safety·2026

Related Experiment Video

Updated: Jun 16, 2026

Construction and Systematical Symmetric Studies of a Series of Supramolecular Clusters with Binary or Ternary Ammonium Triphenylacetates
06:35

Construction and Systematical Symmetric Studies of a Series of Supramolecular Clusters with Binary or Ternary Ammonium Triphenylacetates

Published on: February 15, 2016

A hydrogen bonding motif for forming extended assemblies.

Jiahui Zhang1, Xiangxiang Wu, Kazuhiro Yamato

  • 1College of Chemistry, Beijing Normal University, Beijing 100875, China.

Chemical Communications (Cambridge, England)
|February 4, 2010
PubMed
Summary

Oligoamide strands with tertiary amide groups form H-bonded assemblies. This basic structural motif drives the creation of chain-like and tape-like supramolecular structures.

More Related Videos

Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures
08:15

Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures

Published on: June 26, 2020

Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles
10:23

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

Published on: May 8, 2015

Related Experiment Videos

Last Updated: Jun 16, 2026

Construction and Systematical Symmetric Studies of a Series of Supramolecular Clusters with Binary or Ternary Ammonium Triphenylacetates
06:35

Construction and Systematical Symmetric Studies of a Series of Supramolecular Clusters with Binary or Ternary Ammonium Triphenylacetates

Published on: February 15, 2016

Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures
08:15

Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures

Published on: June 26, 2020

Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles
10:23

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

Published on: May 8, 2015

Area of Science:

  • Supramolecular Chemistry
  • Organic Chemistry
  • Materials Science

Background:

  • Tertiary amide groups are key functional components in various organic molecules.
  • Supramolecular assemblies are formed through non-covalent interactions, influencing material properties.

Purpose of the Study:

  • To identify the fundamental structural features of oligoamide strands that dictate self-assembly.
  • To understand the role of tertiary amide groups in the formation of ordered supramolecular structures.

Main Methods:

  • Synthesis of oligoamide strands with varying tertiary amide group placements.
  • Characterization of self-assembled structures using techniques like X-ray diffraction and spectroscopy.
  • Computational modeling to elucidate the driving forces behind assembly.

Main Results:

  • A conserved structural motif within oligoamide strands was identified.
  • This motif facilitates the formation of hydrogen-bonded (H-bonded) networks.
  • The H-bonded networks lead to the emergence of chain-like or tape-like supramolecular assemblies.

Conclusions:

  • Oligoamide strands featuring tertiary amide groups possess an inherent ability to self-assemble.
  • The identified structural motif is crucial for directing the formation of ordered H-bonded supramolecular architectures.
  • These findings provide insights into the design principles for novel self-assembling materials.