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: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

1.3K
Spin systems where the difference in chemical shifts of the coupled nuclei is greater than ten times J are called first-order spin systems. These nuclei are weakly coupled, and their chemical shifts and coupling constant can generally be estimated from the well-separated signals in the spectrum.
As Δν decreases and the signals move closer, the doublets appear increasingly distorted. The intensities of the inner lines increase at the cost of those of the outer lines as the signals are...
1.3K
2D NMR: Overview of Homonuclear Correlation Techniques01:16

2D NMR: Overview of Homonuclear Correlation Techniques

801
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...
801
NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

3.4K
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...
3.4K
Chemical Shift: Internal References and Solvent Effects01:17

Chemical Shift: Internal References and Solvent Effects

1.5K
In an NMR sample, precise measurement of the absolute absorption frequencies of nuclei is difficult. A standard internal reference compound is added, and the frequency difference between the reference signal and sample signals is measured.
The internal reference compound generally used in NMR spectroscopy is tetramethylsilane (TMS). TMS is preferred because it is chemically inert, soluble in NMR solvents, and easily removable. Also, the highly shielded methyl protons in TMS yield an intense...
1.5K
NMR Spectrometers: Overview01:20

NMR Spectrometers: Overview

2.0K
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...
2.0K
2D NMR: Homonuclear Correlation Spectroscopy (COSY)01:06

2D NMR: Homonuclear Correlation Spectroscopy (COSY)

1.9K
Homonuclear correlation spectroscopy, or COSY, is a 2-dimensional NMR technique that provides information about coupled protons. Typically, the geminal and vicinal coupling are observed. For example, consider the COSY spectrum of ethyl acetate, where its 1D proton NMR spectrum is plotted along the vertical and horizontal axes with their corresponding chemical shift scale. Three spots on the diagonal corresponding to the three peaks in the 1D proton spectrum are called diagonal peaks. The COSY...
1.9K

You might also read

Related Articles

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

Sort by
Same author

A Lipid-Conjugation Strategy for Intracellular Reactive Oxygen Species Control in Hepatic Cells.

Angewandte Chemie (International ed. in English)·2026
Same author

<sup>1</sup>H-<sup>1</sup>H Interatomic Distances in Paracetamol-Based Structures Unveiled by Double-Quantum NMR and DFT Calculations.

Molecules (Basel, Switzerland)·2026
Same author

Moving NMR infrastructures to remote access capabilities.

Progress in nuclear magnetic resonance spectroscopy·2026
Same author

Accordion-like tuning of composite pulse dipolar recoupling in solid-state NMR.

The Journal of chemical physics·2026
Same author

Mobility of lactose in Milk powders.

Food research international (Ottawa, Ont.)·2026
Same author

Boron-Rich Soft Hydrogels Based on the Coassembly of Cationic A‑B‑A Triblock Copolymers with <i>Closo</i>-Dodecaborate.

Macromolecules·2026
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: Apr 26, 2026

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

4.8K

Computer-intensive simulation of solid-state NMR experiments using SIMPSON.

Zdeněk Tošner1, Rasmus Andersen2, Baltzar Stevensson3

  • 1Center for Insoluble Protein Structures (inSPIN), Interdisciplinary Nanoscience Center (iNANO) and Department of Chemistry, Aarhus University, Gustav Wieds Vej 14, DK-8000 Aarhus C, Denmark; NMR Laboratory, Department of Chemistry, Faculty of Science, Charles University in Prague, Hlavova 8, CZ-128 43, Czech Republic.

Journal of Magnetic Resonance (San Diego, Calif. : 1997)
|August 6, 2014
PubMed
Summary
This summary is machine-generated.

This study enhances the SIMPSON NMR software for faster solid-state Nuclear Magnetic Resonance (NMR) simulations on modern hardware. The improved software accelerates complex simulations, aiding in experimental design and spectral analysis.

Keywords:
Cloud computingFast powder averagingOptimal control pulse sequence optimizationSIMPSONSimulation of solid-state NMR experiments

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
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

Related Experiment Videos

Last Updated: Apr 26, 2026

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

4.8K
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
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

Area of Science:

  • Computational chemistry
  • Magnetic resonance spectroscopy

Background:

  • Large-scale solid-state Nuclear Magnetic Resonance (NMR) simulations are computationally intensive.
  • Efficient simulations are crucial for analyzing complex spin systems and designing experiments.

Purpose of the Study:

  • To present an upgraded version of the open-source SIMPSON NMR simulation software.
  • To optimize SIMPSON for high-performance computing (HPC) hardware.

Main Methods:

  • Implemented advanced parallelization techniques for multi-core processors and clusters.
  • Integrated novel interpolation methods (Alderman, Solum, Grant, Wigner transform) for powder averaging.
  • Enhanced optimal control toolbox with higher precision gradients and L-BFGS optimization algorithm.

Main Results:

  • Achieved significant time reductions in solid-state NMR simulations.
  • Demonstrated improved performance on stand-alone computers, multi-core processors, and HPC clusters.
  • Validated the efficiency and novel features through representative simulations.

Conclusions:

  • The enhanced SIMPSON software efficiently accommodates large-scale solid-state NMR simulations.
  • The updated package reflects current advancements in numerical simulation techniques for NMR.
  • This provides a valuable tool for researchers in solid-state NMR spectroscopy.