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

Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
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...
Applications Of NMR In Biology01:25

Applications Of NMR In Biology

Nuclear magnetic resonance (NMR) spectroscopy is a very valuable analytical technique for researchers. It has been used for more than 50 years as an analytical tool. F. Bloch and E. Purcell formulated NMR in 1946 and won the 1952 Nobel Prize in Physics  for their work. Biological macromolecules such as proteins, nucleic acids, lipids, and organic molecules including pharmaceutical compounds, can be studied using this versatile tool that exploits the magnetic properties of certain nuclei.
The...

You might also read

Related Articles

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

Sort by
Same author

DEEP Phaser: A Deep Learning Tandem Vision Transformer for Fully Automated NMR Phase Correction.

The journal of physical chemistry letters·2026
Same author

A fluorescent-protein spin qubit.

Nature·2025
Same author

Detection of intramolecular protein dynamics on nanosecond-to-microsecond timescales by nanoparticle-assisted NMR spin relaxation (NASR).

Nature protocols·2025
Same author

COLMAR1d2d: Synergistic Combination of 1D with 2D NMR for Enhanced High-Throughput Identification and Quantification of Metabolites in Complex Mixtures.

Analytical chemistry·2025
Same author

Dynamics of Globular Proteins when Interacting with Zwitterionic Silica Nanoparticles by Nuclear Magnetic Resonance Spin Relaxation.

Journal of the American Chemical Society·2025
Same author

Coil-Library-Derived Amino-Acid-Specific Side-Chain χ<sub>1</sub> Dihedral Angle Potentials for AMBER-Type Protein Force Field.

Journal of chemical theory and computation·2024
Same journal

Real-Time Vibrational Spectroscopy Reveals an Inversion Transition State in the Photoisomerization of Phenylazoimidazole.

The journal of physical chemistry letters·2026
Same journal

Precursor-Directed Self-Assembly in Hydrothermal Carbon Nitride Nanostructures Revealed by Nano-FTIR.

The journal of physical chemistry letters·2026
Same journal

Correction to "Equation-of-Motion Block-Correlated Coupled Cluster Method for Excited Electronic States of Strongly Correlated Systems".

The journal of physical chemistry letters·2026
Same journal

Rationalizing Stacking-Dependent Charge Injection Dynamics in Radical-Based Organic Light-Emitting Diodes.

The journal of physical chemistry letters·2026
Same journal

Bottom-Up Formation of the Simplest Geminal Thiol─Methanedithiol (CH<sub>2</sub>(SH)<sub>2</sub>)─and the Methyl Hydrodisulfide (H<sub>3</sub>CSSH) Isomer in Interstellar Analogue Ices.

The journal of physical chemistry letters·2026
Same journal

Trion Mediated Sequential Charge Separation in Functionalized CsPbBr<sub>3</sub>/AgInS<sub>2</sub> Hybrid Nanocrystals.

The journal of physical chemistry letters·2026
See all related articles

Related Experiment Video

Updated: May 13, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
09:25

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

Gel-Based NMR Method for Observing Submicrosecond Protein Dynamics at Atomic Resolution.

Xinyao Xiang1, Mamata Basnet1, Mouzhe Xie2

  • 1Department of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio 43210, United States.

The Journal of Physical Chemistry Letters
|May 12, 2026
PubMed
Summary
This summary is machine-generated.

Researchers enhanced nuclear magnetic resonance (NMR) methods to study protein dynamics. Using gels instead of nanoparticles, they expanded the observable timescale for protein motions, offering new insights into molecular dynamics.

More Related Videos

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

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the &#181;s-ms Timescale
08:09

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale

Published on: April 19, 2021

Related Experiment Videos

Last Updated: May 13, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
09:25

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

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

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the &#181;s-ms Timescale
08:09

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale

Published on: April 19, 2021

Area of Science:

  • Biochemistry
  • Biophysics
  • Structural Biology

Background:

  • Nuclear Magnetic Resonance (NMR) spectroscopy is vital for studying protein dynamics.
  • Existing NMR relaxation methods are limited to fast timescales (subnanosecond to nanosecond).
  • Nanoparticle-assisted spin relaxation (NASR) extends this window but requires specific reagents.

Purpose of the Study:

  • To generalize the NASR method using readily available gels.
  • To investigate submicrosecond protein dynamics using gel-induced relaxation enhancement.
  • To complement existing NMR techniques for characterizing protein motion.

Main Methods:

  • Utilized polyacrylamide and agarose gels to induce transverse relaxation enhancement (ΔR2) in NMR.
  • Measured ΔR2 changes in the presence of compressed and uncompressed gels.
  • Applied the generalized NASR approach to K-Ras and other proteins.

Main Results:

  • Demonstrated that gels induce a measurable transverse relaxation enhancement (ΔR2).
  • Showed ΔR2 is proportional to the site-specific order parameter (S2), reflecting submicrosecond dynamics.
  • Successfully applied the method to diverse proteins with complex dynamics.

Conclusions:

  • Gel-induced transverse relaxation enhancement provides a generalized and accessible method for studying protein dynamics.
  • This technique expands the accessible timescale for NMR dynamics studies into the submicrosecond range.
  • The method offers complementary information to existing NMR dynamics approaches, particularly for K-Ras.