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

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...
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-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...
Intermolecular Forces03:13

Intermolecular Forces

Atoms and molecules interact through bonds (or forces): intramolecular and intermolecular. The forces are electrostatic as they arise from interactions (attractive or repulsive) between charged species (permanent, partial, or temporary charges) and exist with varying strengths between ions, polar, nonpolar, and neutral molecules. The different types of intermolecular forces are ion–dipole, dipole–dipole, hydrogen bonds, and dispersion; among these, dipole–dipole, hydrogen bonds, and dispersion...
Intermolecular Forces03:13

Intermolecular Forces

Atoms and molecules interact through bonds (or forces): intramolecular and intermolecular. The forces are electrostatic as they arise from interactions (attractive or repulsive) between charged species (permanent, partial, or temporary charges) and exist with varying strengths between ions, polar, nonpolar, and neutral molecules. The different types of intermolecular forces are ion–dipole, dipole–dipole, hydrogen bonds, and dispersion; among these, dipole–dipole, hydrogen bonds, and dispersion...

You might also read

Related Articles

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

Sort by
Same author

Open- and Closed-Shell Roles of Sensitizer and Annihilator in Pseudo-Single Component Mixtures for Upconversion.

Journal of the American Chemical Society·2026
Same author

Lanthanide-doped nanocrystals enable organic room-temperature phosphorescence in solution through direct triplet excitation.

Nature chemistry·2026
Same author

Coulombic control of charge transfer in radicals with quartet recycling luminescence.

Nature communications·2026
Same author

On the Design of Steep Optical Absorbers for Vacuum-Processed Organic Solar Cells: One Isopropyl Group Makes the Difference.

Small science·2026
Same author

Mechanistic insights into azo compound back-isomerization from spin-flip time-dependent DFT combined with Marcus theory.

Chemical science·2026
Same author

Bioinspired Strategies for Directional Water Transport in Asymmetric Membranes.

ACS applied polymer materials·2026

Related Experiment Video

Updated: Jun 4, 2026

Molecular Spring Constant Analysis by Biomembrane Force Probe Spectroscopy
08:10

Molecular Spring Constant Analysis by Biomembrane Force Probe Spectroscopy

Published on: November 20, 2021

Force Reveals Hidden Conformations and Dissociation Pathways in Individual π-Interacting Dimers.

Célia Franceschini1, Dorothée Brandt2, Maxime Ledent1

  • 1Research Unit Molsys, NanoChem, University of Liège, Liège, Belgium.

Angewandte Chemie (International Ed. in English)
|June 3, 2026
PubMed
Summary

Mechanical force controls molecular structure using noncovalent interactions. Atomic force microscopy revealed hidden parallel and anti-parallel perylene diimide conformers, detailing their distinct mechanical stability and rupture pathways.

Keywords:
AFMconformational dynamicsmechanochemical pathwaysnoncovalent interactionssingle‐molecule force spectroscopy

More Related Videos

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates
06:48

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates

Published on: January 5, 2024

Force Spectroscopy of Single Protein Molecules Using an Atomic Force Microscope
06:45

Force Spectroscopy of Single Protein Molecules Using an Atomic Force Microscope

Published on: February 28, 2019

Related Experiment Videos

Last Updated: Jun 4, 2026

Molecular Spring Constant Analysis by Biomembrane Force Probe Spectroscopy
08:10

Molecular Spring Constant Analysis by Biomembrane Force Probe Spectroscopy

Published on: November 20, 2021

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates
06:48

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates

Published on: January 5, 2024

Force Spectroscopy of Single Protein Molecules Using an Atomic Force Microscope
06:45

Force Spectroscopy of Single Protein Molecules Using an Atomic Force Microscope

Published on: February 28, 2019

Area of Science:

  • Supramolecular Chemistry
  • Materials Science
  • Chemical Physics

Background:

  • Mechano-responsive materials leverage mechanical force to alter molecular structure.
  • Noncovalent interactions offer tunable mechanical stability and reversibility.
  • Conventional ensemble techniques struggle to access conformational energy landscapes of noncovalent motifs.

Purpose of the Study:

  • To probe individual π-interactions within a perylene diimide dimer using single-molecule force spectroscopy.
  • To reveal hidden conformational states and map their force-dependent energy landscape.
  • To provide molecular-level insight into the mechanics of π-π interactions.

Main Methods:

  • Atomic force microscopy (AFM)-based force spectroscopy (single-molecule pulling experiments).
  • Molecular dynamics (MD) simulations, including steered MD.
  • Passive force spectroscopy for real-time conformer resolution.

Main Results:

  • Two distinct, long-lived conformers (parallel and anti-parallel perylene diimide orientations) were identified, previously indistinguishable by ensemble methods.
  • The parallel conformer showed greater mechanical stability and a sequential rupture pathway involving interconversion to the anti-parallel state.
  • Passive force spectroscopy validated the force-induced interconversion pathway and quantified mechanical properties.

Conclusions:

  • Combining passive force spectroscopy with MD simulations can uncover hidden conformational states in noncovalent assemblies.
  • This approach maps the force-dependent energy landscape of supramolecular systems.
  • Single-molecule force spectroscopy is a powerful tool for understanding the mechanics of π-π interactions and other noncovalent bonds.