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

2D NMR: Overview of Homonuclear Correlation Techniques01:16

2D NMR: Overview of Homonuclear Correlation Techniques

811
Homonuclear correlation spectroscopy (COSY) is a powerful technique used in Nuclear Magnetic Resonance (NMR) spectroscopy to study the correlations between nuclei of the same type within a molecule. It provides information about scalar couplings between adjacent nuclei, which helps determine connectivity and structural information. There are several COSY variants, each with its unique strengths and experimental parameters.
COSY90 is the standard two-dimensional (2D) COSY experiment that...
811
NMR Spectrometers: Resolution and Error Correction01:14

NMR Spectrometers: Resolution and Error Correction

999
When magnetic nuclei in a sample achieve resonance and undergo relaxation, the signal detected in NMR is an approximately exponential free induction decay. Fourier transform of an exponential decay yields a Lorentzian peak in the frequency domain. Lorentzian peaks in an NMR spectrum are defined by their amplitude, full width at half maximum, and position, where the peak width is governed by the spin-spin relaxation time alone. In real experiments, however, the applied magnetic field is rendered...
999
2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)01:19

2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)

1.3K
Heteronuclear single-quantum correlation spectroscopy (HSQC) is a 2D NMR technique that reveals one-bond correlations between hydrogen and a heteronucleus. The HSQC experiment is similar to the heteronuclear correlation experiment (HETCOR) but is more sensitive. In the HSQC spectrum, the proton chemical shift is plotted on the horizontal F2 axis, while the 13C chemical shift is plotted on the vertical F1 axis. The corresponding proton and 13C spectra are also shown. The HSQC contour plot does...
1.3K
Two-Dimensional (2D) NMR: Overview01:12

Two-Dimensional (2D) NMR: Overview

1.6K
The 1D NMR spectrum of large and complex molecules like natural products has complicated splitting patterns and overlapping signals, which can be easily interpreted using 2-dimensional (2D) NMR. Unlike 1D NMR, 2D NMR has two frequency axes that provide the coupling information between the nucleus A and nucleus B in a molecule. The process from which 2D spectra are obtained has four steps.
The first step is the preparation period, during which nucleus A is excited with a radiofrequency pulse....
1.6K
NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

3.5K
The spin state of an NMR-active nucleus can have a slight effect on its immediate electronic environment. This effect propagates through the intervening bonds and affects the electronic environments of NMR-active nuclei up to three bonds away; occasionally, even farther. This phenomenon is called spin–spin coupling or J-coupling. Coupling interactions are mutual and result in small changes in the absorption frequencies of both nuclei involved. While nuclei of the same element are involved...
3.5K
NMR Spectrometers: Overview01:20

NMR Spectrometers: Overview

2.1K
NMR spectrometers consist of a strong magnet, a radiofrequency transmitter, and a detector attached to a computer console for recording spectra of samples containing NMR-active nuclei. In first-generation NMR instruments called continuous-wave spectrometers, the resonance frequencies of the nuclei are determined by frequency-sweep or field-sweep methods. The magnetic field strength is fixed and the rf signal is swept in the former, while the radiofrequency signal is fixed and the magnetic field...
2.1K

You might also read

Related Articles

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

Sort by
Same author

A neutral multivalent AIE-TICT scaffold: An off-on, wash-free fluorogenic strategy for biosensing glycan-protein interactions in live cells and mycobacteria.

Analytica chimica acta·2025
Same author

Predicting the T790M mutation in non-small cell lung cancer (NSCLC) using brain metastasis MR radiomics: a study with an imbalanced dataset.

Discover oncology·2024
Same author

Assessment of cellular responses in three-dimensional cell cultures through chemical exchange saturation transfer and <sup>1</sup> H MRS.

NMR in biomedicine·2023
Same author

The Application of DTCWT on MRI-Derived Radiomics for Differentiation of Glioblastoma and Solitary Brain Metastases.

Journal of personalized medicine·2022
Same author

Magnetically Aligned Lipid Bilayers with High Cholesterol for Solid-State NMR of Membrane Proteins.

Biochemistry·2022
Same author

Chemical Exchange Saturation Transfer (CEST) Signal at -1.6 ppm and Its Application for Imaging a C6 Glioma Model.

Biomedicines·2022
Same journal

Localization-driven exchange contrast in diffusion exchange spectroscopy.

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

4.5 Tesla superconducting miniature magnet in liquid nitrogen.

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

Folding and unfolding dynamics of a DNA aptamer studied by heteronuclear <sup>1</sup>H-<sup>13</sup>C correlation zz-exchange spectroscopy.

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

Multi-spin control from one-spin pulses.

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

Altering MRI rotating frame relaxations by changing the truncation level of Hyperbolic Secant pulse.

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

Effects of proton exchange on the lifetimes of long-lived states in aliphatic chains.

Journal of magnetic resonance (San Diego, Calif. : 1997)·2026
See all related articles

Related Experiment Video

Updated: May 6, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

16.8K

Sampling scheme and compressed sensing applied to solid-state NMR spectroscopy.

Eugene C Lin1, Stanley J Opella1

  • 1Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093-0307, United States.

Journal of Magnetic Resonance (San Diego, Calif. : 1997)
|October 22, 2013
PubMed
Summary
This summary is machine-generated.

Non-uniform sampling compressed sensing significantly reduces data requirements for solid-state NMR. This technique allows high-fidelity reconstruction of 2D and 3D spectra using only 25-33% of a full dataset.

Keywords:
Compressed sensingMembrane proteinsNon-uniform samplingOriented samplesProtein NMRSensitivitySolid-state NMR

More Related Videos

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy NMR and Microscale Thermophoresis MST
10:28

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy NMR and Microscale Thermophoresis MST

Published on: November 2, 2018

13.5K
Multiplex Chemical Imaging Based on Broadband Stimulated Raman Scattering Microscopy
09:57

Multiplex Chemical Imaging Based on Broadband Stimulated Raman Scattering Microscopy

Published on: July 25, 2022

3.8K

Related Experiment Videos

Last Updated: May 6, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

16.8K
Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy NMR and Microscale Thermophoresis MST
10:28

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy NMR and Microscale Thermophoresis MST

Published on: November 2, 2018

13.5K
Multiplex Chemical Imaging Based on Broadband Stimulated Raman Scattering Microscopy
09:57

Multiplex Chemical Imaging Based on Broadband Stimulated Raman Scattering Microscopy

Published on: July 25, 2022

3.8K

Area of Science:

  • Nuclear Magnetic Resonance (NMR) Spectroscopy
  • Materials Science
  • Data Acquisition Techniques

Background:

  • Solid-state NMR is crucial for characterizing materials.
  • Traditional data acquisition in NMR is time-consuming.
  • Compressed sensing offers potential for accelerating data acquisition.

Purpose of the Study:

  • To integrate non-uniform sampling compressed sensing with solid-state NMR.
  • To evaluate the efficiency and fidelity of this combined technique for both oriented and unoriented samples.

Main Methods:

  • Incorporation of non-uniform sampling (NUS) compressed sensing (CS) into oriented sample (OS) and magic angle spinning (MAS) solid-state NMR.
  • Utilized both simulated and experimental data for validation.

Main Results:

  • High-fidelity reconstruction of 2D and 3D solid-state NMR spectra achieved with only 25-33% of a full linearly sampled dataset.
  • Demonstrated applicability to both stationary aligned (OS) and unoriented (MAS) samples.
  • Observed a modest increase in signal-to-noise ratio post-reconstruction.

Conclusions:

  • NUS-CS is an effective method for accelerating data acquisition in solid-state NMR.
  • Significant data reduction is possible without compromising spectral quality.
  • This approach enhances the practicality and efficiency of solid-state NMR analysis.