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

992
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...
992
Protein Folding01:25

Protein Folding

8.8K
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...
8.8K
Protein Folding01:22

Protein Folding

112.3K
Overview
112.3K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

1.8K
1.8K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

2.3K
2.3K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

7.4K
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...
7.4K

You might also read

Related Articles

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

Sort by
Same author

Correction: YTHDF2 in peritumoral hepatocytes mediates chemotherapy-induced antitumor immune responses through CX3CL1-mediated CD8<sup>+</sup> T cell recruitment.

Molecular cancer·2026
Same author

Entropic Charge Separation as a General Mechanism Arresting Nanoscale Condensate Coarsening.

Physical review letters·2026
Same author

Deviation analysis of guided fiber post removal using an assembled sleeveless guide system: A case series.

The Journal of prosthetic dentistry·2026
Same author

Sticky enzymes: increased metabolic efficiency via substrate-dependent enzyme clustering.

PRX life·2026
Same author

Conformational Entropy of Intrinsically Disordered Proteins Bars Intruders from Biomolecular Condensates.

PRX life·2026
Same author

Angiographic Quantitative Flow Ratio-Guided Coronary Intervention: 5-Year Follow-Up From the FAVOR III China Randomized Trial.

Journal of the American College of Cardiology·2026

Related Experiment Video

Updated: May 1, 2026

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

16.2K

Conformational dynamics through an intermediate.

Ashok Garai1, Yaojun Zhang1, Olga K Dudko1

  • 1Department of Physics and Center for Theoretical Biological Physics, University of California at San Diego, La Jolla, California 92093, USA.

The Journal of Chemical Physics
|April 10, 2014
PubMed
Summary
This summary is machine-generated.

Understanding intermediate states in nanostructure self-assembly is crucial. This study provides a statistical mechanical model to analyze conformational dynamics under force, revealing kinetics and barriers.

More Related Videos

Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling
11:55

Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling

Published on: May 29, 2011

17.2K
Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
08:03

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Published on: April 13, 2022

1.8K

Related Experiment Videos

Last Updated: May 1, 2026

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

16.2K
Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling
11:55

Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling

Published on: May 29, 2011

17.2K
Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
08:03

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Published on: April 13, 2022

1.8K

Area of Science:

  • * Biophysics and statistical mechanics
  • * Nanotechnology and self-assembly

Background:

  • * Biological and synthetic nanostructures often form through intermediate states.
  • * These intermediates critically influence functional or detrimental outcomes in living systems.
  • * Understanding conformational dynamics is key to controlling self-assembly.

Purpose of the Study:

  • * To develop a statistical mechanical framework for conformational dynamics through intermediates under variable force.
  • * To derive an analytical solution for the force distribution at conformational transitions.
  • * To enable precise characterization of intermediate states in self-assembly.

Main Methods:

  • * Applied statistical mechanics to model conformational dynamics.
  • * Analyzed systems undergoing transitions under variable external force.
  • * Derived an analytical solution for the force-dependent transition probability.

Main Results:

  • * Developed a model for conformational dynamics through intermediates under force.
  • * Derived an analytical solution for the force distribution at transitions.
  • * Revealed complex kinetics across a wide parameter range.
  • * Enabled localization of intermediates and extraction of kinetic parameters.

Conclusions:

  • * The developed model accurately describes conformational dynamics through intermediates.
  • * The analytical solution provides a powerful tool for analyzing experimental data.
  • * This work facilitates the characterization of intermediate states and their associated energy landscapes.