Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Protein Dynamics in Living Cells

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 Labile Protons: Temporal Resolution

¹H NMR of Labile Protons: Temporal Resolution

Protons bonded to heteroatoms such as nitrogen and oxygen exhibit a range of chemical shift values. This is due to the varying degree of hydrogen bonding between the proton and the heteroatom in other molecules. The extent of hydrogen bonding affects the electron density around the proton, thereby giving different chemical shift values for the protons in the proton NMR spectrum.
The –OH proton in alcohols typically appears in the range of δ 2 to 5 ppm but can vary depending on the specific...

Applications Of NMR In Biology

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...

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

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...

You might also read

Related Articles

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

Sort by

Same author

The Effect of Protein Tagging on Aggregation and Phase Separation.

Journal of cellular biochemistry·2026

Same author

Mechanically stable high-sensitivity Rheo-NMR spectroscopy for real-time monitoring of shear-induced phase transitions.

Journal of magnetic resonance (San Diego, Calif. : 1997)·2026

Same author

Leucyl-tRNA synthetase as a molecular target of isobutanol-mediated growth inhibition in Saccharomyces cerevisiae.

The Journal of biological chemistry·2026

Same author

Structure-Guided Grafting of Cell-Penetrating Motifs into Stapled Peptides for Intracellular PPI Inhibition.

Journal of medicinal chemistry·2026

Same author

Backbone resonance assignments of CPEB3 [1-120], CPEB3 [186-315], and CPEB3 [400-459].

Biomolecular NMR assignments·2026

Same author

Degradation mechanism of the von Willebrand factor A2 domain by nattokinase.

FEBS letters·2026

Search research articles

Related Experiment Video

Updated: May 28, 2026

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

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

Published on: November 1, 2024

Boosting protein dynamics studies using quantitative nonuniform sampling NMR spectroscopy.

Yoh Matsuki¹, Tsuyoshi Konuma, Toshimichi Fujiwara

¹Institute for Protein Research, Osaka University, Osaka, Japan.

The Journal of Physical Chemistry. B

|October 14, 2011

Summary

This summary is machine-generated.

This study enhances Nuclear Magnetic Resonance (NMR) relaxation measurements using advanced processing. The improved method significantly accelerates data collection for protein dynamics studies, enabling analysis of challenging samples.

More Related Videos

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Published on: April 13, 2022

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

Published on: April 28, 2022

Related Experiment Videos

Last Updated: May 28, 2026

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

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

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Published on: April 13, 2022

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

Published on: April 28, 2022

Area of Science:

Biophysics
Structural Biology
Biochemistry

Background:

Nuclear Magnetic Resonance (NMR) spectroscopy offers atomic resolution for protein dynamics.
Traditional NMR relaxation measurements are time-consuming, limiting studies on transient biological samples.
Non-uniform sampling (NUS) in NMR is recognized for efficiency but challenging for quantitative relaxation analysis.

Purpose of the Study:

To enhance the SIFT (Spectroscopy by Integration of Frequency and Time domain information) processing method for NUS NMR.
To enable accelerated and accurate quantitative NMR relaxation measurements.
To demonstrate the application of improved SIFT processing for protein dynamics studies.

Main Methods:

Development of an advanced SIFT processing algorithm with increased frequency domain information utilization.
Application of the enhanced SIFT method to R(2) relaxation dispersion measurements.
Utilized the KIX domain of mouse CREB-binding protein (CBP) as a model system.

Main Results:

The enhanced SIFT processing significantly accelerates quantitative NMR relaxation measurements.
Achieved a 10-fold expedition in R(2) relaxation dispersion measurements for the KIX domain of CBP.
Demonstrated preservation of analytical accuracy with accelerated data acquisition.

Conclusions:

The advanced SIFT processing method is crucial for accelerating NMR relaxation measurements while maintaining accuracy.
This quantitative NUS processing enables faster studies of protein dynamics, even for short-lived samples.
The improved SIFT approach is broadly applicable to various NMR relaxation measurements.