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

Mechanical Protein Functions01:58

Mechanical Protein Functions

5.2K
Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force. 
5.2K
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

957
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...
957
Protein Folding01:25

Protein Folding

9.7K
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...
9.7K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

18.7K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
18.7K
Mechanisms of Membrane-bending01:15

Mechanisms of Membrane-bending

3.0K
The living membranes are flexible due to their fluid mosaic nature; however, their bending into different shapes is an active process regulated by specific lipids and proteins. The membrane bending can be transient as seen in vesicles or stable for a long time as in microvilli. Cells regulate the size, location, and duration of the membrane curvature.
Membrane bending can happen due to intrinsic changes in lipid composition or extrinsic association with different proteins. The proteins involved...
3.0K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

2.5K
2.5K

You might also read

Related Articles

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

Sort by
Same author

Efficient sampling of large-scale transition pathways and intermediate conformations in sub-mesoscopic protein complexes.

Nature communications·2026
Same author

Uniaxial Tensile Tests and Digital Image Correlation Analysis for the Mechanical Characterization of Human Fascia Lata Under Different Decellularization Treatments.

Journal of biomedical materials research. Part A·2025
Same author

The 15th Anniversary of <i>Materials</i>-Recent Advances in Advanced Materials Characterization.

Materials (Basel, Switzerland)·2025
Same author

Sound Sensing: Generative and Discriminant Model-Based Approaches to Bolt Loosening Detection.

Sensors (Basel, Switzerland)·2024
Same author

Fatigue Characteristics of 7050-T7451 Aluminum Alloy Friction Stir Welding Joints and the Stress Ratio Effect.

Materials (Basel, Switzerland)·2022
Same author

Design and Mechanical Characterization Using Digital Image Correlation of Soft Tissue-Mimicking Polymers.

Polymers·2022
Same journal

RETRACTED: Kim et al. The Angiogenesis Inhibitor ALS-L1023 from Lemon-Balm Leaves Attenuates High-Fat Diet-Induced Nonalcoholic Fatty Liver Disease Through Regulating the Visceral Adipose-Tissue Function. <i>Int. J. Mol. Sci.</i> 2017, <i>18</i>, 846.

International journal of molecular sciences·2026
Same journal

Correction: Mahmud et al. Thymoquinone Attenuates NF-κβ Signalling Activation in Retinal Pigment Epithelium Cells Under AMD-Mimicking Conditions. <i>Int. J. Mol. Sci.</i> 2025, <i>26</i>, 11473.

International journal of molecular sciences·2026
Same journal

Correction: Borovikov et al. The Twisting and Untwisting of Actin and Tropomyosin Filaments Are Involved in the Molecular Mechanisms of Muscle Contraction, and Their Disruption Can Result in Muscle Disorders. <i>Int. J. Mol. Sci</i>. 2025, <i>26</i>, 6705.

International journal of molecular sciences·2026
Same journal

Correction: Molagoda et al. Flavonoid Glycosides from <i>Ziziphus jujuba</i> var. <i>inermis</i> (Bunge) Rehder Seeds Inhibit α-Melanocyte-Stimulating Hormone-Mediated Melanogenesis. <i>Int. J. Mol. Sci.</i> 2021, <i>22</i>, 7701.

International journal of molecular sciences·2026
Same journal

Correction: Guo et al. Integrated Transcriptomic and Metabolomic Analysis Reveals the Molecular Regulatory Mechanism of Flavonoid Biosynthesis in Maize Roots Under Lead Stress. <i>Int. J. Mol. Sci.</i> 2024, <i>25</i>, 6050.

International journal of molecular sciences·2026
Same journal

Correction: Chang et al. Improvement of Carbon Tetrachloride-Induced Acute Hepatic Failure by Transplantation of Induced Pluripotent Stem Cells Without Reprogramming Factor c-Myc. <i>Int. J. Mol. Sci.</i> 2012, <i>13</i>, 3598-3617.

International journal of molecular sciences·2026
See all related articles

Related Experiment Video

Updated: Oct 17, 2025

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States
04:37

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States

Published on: June 29, 2021

2.9K

Low-Frequency Harmonic Perturbations Drive Protein Conformational Changes.

Domenico Scaramozzino1, Gianfranco Piana1,2, Giuseppe Lacidogna1

  • 1Department of Structural, Geotechnical and Building Engineering, Politecnico di Torino, Corso Duca degli Abruzzi 24, 10129 Torino, Italy.

International Journal of Molecular Sciences
|October 13, 2021
PubMed
Summary
This summary is machine-generated.

Protein dynamics, crucial for function, can be predicted using elastic network models (ENMs). This study shows low-frequency dynamic perturbations can trigger protein conformational changes, suggesting external collisions play a role.

Keywords:
conformational changeelastic network modelharmonic perturbationlow-frequency vibrationsmodal analysisprincipal component analysisprotein dynamics

More Related Videos

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
09:25

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

Published on: November 1, 2024

2.2K
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

2.3K

Related Experiment Videos

Last Updated: Oct 17, 2025

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States
04:37

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States

Published on: June 29, 2021

2.9K
Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
09:25

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

Published on: November 1, 2024

2.2K
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

2.3K

Area of Science:

  • Biophysics
  • Computational Biology

Background:

  • Protein dynamics are key to understanding the link between structure and function.
  • Elastic network models (ENMs) are established tools for predicting protein flexibility and conformational changes.
  • Existing ENM methods typically analyze free vibrations or static perturbations.

Purpose of the Study:

  • To integrate free vibration and static perturbation approaches in ENMs.
  • To evaluate the complete protein response to dynamic perturbations.
  • To investigate the role of low-frequency dynamics in protein conformational changes.

Main Methods:

  • Applied harmonic forces simulating particle collisions to protein ENMs.
  • Solved dynamic equations in the underdamped regime, considering mass, damping, and stiffness.
  • Analyzed protein motion in coordinate and principal component spaces.

Main Results:

  • Dynamic perturbations, particularly in the low-frequency range, effectively drive protein conformational changes.
  • High direction similarity was observed between applied perturbations and resulting motions.
  • The study demonstrates a connection between external dynamic forces and protein structural rearrangements.

Conclusions:

  • Protein conformational changes may be initiated by external collisions.
  • The inherent low-frequency dynamics of protein structures facilitate these conformational changes.
  • This integrated ENM approach offers a more comprehensive view of protein dynamics and function.