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

Bond Dissociation Energy and Activation Energy02:13

Bond Dissociation Energy and Activation Energy

Bond energy is the energy required to break a bond homolytically. These values are usually expressed in units of kcal/mol or kJ/mol and are referred to as bond dissociation energies when given for specific bonds or average bond energies when indicated for a given type of bond over many compounds. Firstly, the bond dissociation energy for a single bond is weaker than that of a double bond, which in turn is weaker than that of a triple bond. Secondly, hydrogen forms relatively strong bonds with...
IR Spectroscopy: Hooke's Law Approximation of Molecular Vibration01:16

IR Spectroscopy: Hooke's Law Approximation of Molecular Vibration

A covalently bonded heteronuclear diatomic molecule can be modeled as two vibrating masses connected by a spring. The vibrational frequency of the bond can be expressed using an equation derived from Hooke's law, which describes how the force applied to stretch or compress a spring is proportional to the displacement of the spring. In this case, the atoms behave like masses, and the bond acts like a spring.
According to Hooke's law, the vibrational frequency is directly proportional to the...
Mass Spectrometry: Molecular Fragmentation Overview01:20

Mass Spectrometry: Molecular Fragmentation Overview

The ionization of a molecule into a molecular ion inside the mass spectrometer causes instability in the molecule's structure due to the loss of an electron. This eventually leads to the fragmentation or breaking of some bonds in the molecule. The fragmentation occurs predominantly at specific bonds to yield relatively stable fragments.
One type of fragmentation pattern is the cleavage of a single bond in the molecular ion. The cleavage leads to a radical and a cation. The cleavage can occur at...
Double Resonance Techniques: Overview01:12

Double Resonance Techniques: Overview

Double resonance techniques in Nuclear Magnetic Resonance (NMR) spectroscopy involve the simultaneous application of two different frequencies or radiofrequency pulses to manipulate and observe two distinct nuclear spins. One important application of double resonance is spin decoupling, which selectively suppresses coupling with one type of nucleus while observing the NMR signal from another nucleus, simplifying the spectrum and enhancing resolution.
Spin decoupling is usually achieved by...
¹³C NMR: ¹H–¹³C Decoupling01:04

¹³C NMR: ¹H–¹³C Decoupling

The probability of having two carbon-13 atoms next to each other is negligible because of the low natural abundance of carbon-13. Consequently, peak splitting due to carbon-carbon spin-spin coupling is not observed in spectra. However, protons up to three sigma bonds away split the carbon signal according to the n+1 rule, resulting in complicated spectra.
A broadband decoupling technique is used to simplify these complex, sometimes overlapping, signals. Broadband decoupling relies on a...
Bond Energies and Bond Lengths02:49

Bond Energies and Bond Lengths

Stable molecules exist because covalent bonds hold the atoms together. The strength of a covalent bond is measured by the energy required to break it, that is, the energy necessary to separate the bonded atoms. Separating any pair of bonded atoms requires energy — the stronger a bond, the greater the energy required to break it.

You might also read

Related Articles

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

Sort by
Same author

Targeting intracellular cholesterol imbalance rescues sarcomere-ER contact site signaling and ER remodeling in dilated cardiomyopathy.

Signal transduction and targeted therapy·2026
Same author

Phase-separated plasma membranes show elevated viscosity and reduced line tension of liquid-ordered domains.

Journal of colloid and interface science·2025
Same author

Tissue tension of planar, free standing cell monolayers measured by central deformation.

PNAS nexus·2025
Same author

Nonmuscle Myosin-2B Regulates Apical Cortical Mechanics, ZO-1 Dynamics and Cell Size in MDCK Epithelial Cells.

Cells·2025
Same author

Quaternary Ammonium Salts as Supporting Electrolytes in Cathodic Reductions: An Analysis of Their Electrochemical Stability.

The journal of physical chemistry. B·2025
Same author

A feedback circuitry involving γ-actin, β-actin and nonmuscle myosin-2 A controls tight junction and apical cortex mechanics.

Nature communications·2025

Related Experiment Video

Updated: Jun 27, 2026

Investigating Receptor-ligand Systems of the Cellulosome with AFM-based Single-molecule Force Spectroscopy
11:34

Investigating Receptor-ligand Systems of the Cellulosome with AFM-based Single-molecule Force Spectroscopy

Published on: December 20, 2013

Dynamic force spectroscopy: Analysis of reversible bond-breaking dynamics.

Gregor Diezemann1, Andreas Janshoff

  • 1Institut fur Physikalische Chemie, Universitat Mainz, Welderweg 11, 55099 Mainz, Germany. diezeman@uni-mainz.de

The Journal of Chemical Physics
|December 3, 2008
PubMed
Summary

This study analyzes bond dissociation dynamics under force, revealing how loading rates and rebinding influence rupture forces. Equilibrium constants can be extracted from rupture force measurements, offering insights into molecular interactions.

More Related Videos

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

Fluorescence Biomembrane Force Probe: Concurrent Quantitation of Receptor-ligand Kinetics and Binding-induced Intracellular Signaling on a Single Cell
14:09

Fluorescence Biomembrane Force Probe: Concurrent Quantitation of Receptor-ligand Kinetics and Binding-induced Intracellular Signaling on a Single Cell

Published on: August 4, 2015

Related Experiment Videos

Last Updated: Jun 27, 2026

Investigating Receptor-ligand Systems of the Cellulosome with AFM-based Single-molecule Force Spectroscopy
11:34

Investigating Receptor-ligand Systems of the Cellulosome with AFM-based Single-molecule Force Spectroscopy

Published on: December 20, 2013

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

Fluorescence Biomembrane Force Probe: Concurrent Quantitation of Receptor-ligand Kinetics and Binding-induced Intracellular Signaling on a Single Cell
14:09

Fluorescence Biomembrane Force Probe: Concurrent Quantitation of Receptor-ligand Kinetics and Binding-induced Intracellular Signaling on a Single Cell

Published on: August 4, 2015

Area of Science:

  • Biophysics
  • Chemical Physics

Background:

  • Understanding bond dissociation is crucial for molecular mechanics.
  • Diffusive processes and external forces significantly impact bond stability.

Purpose of the Study:

  • To investigate diffusive bond dissociation in a double well potential under external force.
  • To analyze the influence of finite rebinding probabilities on the dynamic force spectrum.
  • To determine how parameters like loading rate and linker compliance affect rupture forces.

Main Methods:

  • Theoretical modeling of barrier crossing dynamics.
  • Computation of rupture force probability distributions.
  • Analysis of force-dependent bond dynamics under varying external conditions.

Main Results:

  • Rupture and rejoining forces depend on loading rates, consistent with potential shape.
  • At low loading rates, pull and relax modes converge towards equilibrium.
  • Soft linker compliance can either not affect or predictably alter equilibrium rupture force.

Conclusions:

  • Finite rebinding probabilities and loading rates critically influence dynamic force spectra.
  • Equilibrium constants can be determined from equilibrium rupture force measurements.
  • The study provides a framework for understanding and quantifying molecular bond behavior under force.