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Related Concept Videos

NMR Spectroscopy Of Amines01:19

NMR Spectroscopy Of Amines

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In proton NMR spectroscopy, primary amines and secondary amines showcase their N–H protons as a broad signal in the chemical shift range between δ 0.5 and 5 ppm. The exact position in this range depends on several factors, including sample concentration, hydrogen bonding, and the type of solvent used. Since amine protons undergo fast proton exchange in solution, the protons are labile and therefore do not participate in any splitting with adjacent protons. Thus, the observed peak is...
11.1K
NMR Spectroscopy of Aromatic Compounds01:14

NMR Spectroscopy of Aromatic Compounds

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Aromatic compounds can be identified or analyzed using proton NMR and carbon‐13 NMR. Typically, aromatic hydrogens or hydrogens directly bonded to the aromatic rings are strongly deshielded by the aromatic ring current. Therefore, they absorb in the range of 6.5–8.0 ppm in proton NMR spectra. For instance, aromatic hydrogens directly bonded to the benzene ring absorb at 7.3 ppm. However, aromatic hydrogens of larger rings absorb farther upfield or downfield than the ideal range.
6.3K
NMR Spectroscopy of Benzene Derivatives01:34

NMR Spectroscopy of Benzene Derivatives

11.1K
Simple unsubstituted benzene has six aromatic protons, all chemically equivalent. Therefore, benzene exhibits only a singlet peak at δ 7.3 ppm in the 1H NMR spectrum. The observed shift is far downfield because the aromatic ring current strongly deshields the protons. Any substitution on the benzene ring makes the aromatic protons nonequivalent, and the protons split each other. The peak is, therefore, no longer a singlet and the splitting pattern and their associated coupling...
11.1K
NMR Spectroscopy: Chemical Shift Overview01:15

NMR Spectroscopy: Chemical Shift Overview

3.3K
The position of the absorption signal of a sample is reported relative to the position of the signal of tetramethylsilane (TMS), which is added as an internal reference while recording spectra. The difference between the absorption frequencies of the sample and TMS (in Hz) is divided by the spectrometer operating frequency (in MHz) to obtain a dimensionless quantity called the chemical shift. It is reported on the δ (delta) scale and expressed in parts per million.
For instance, the proton...
3.3K
NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

3.2K
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...
3.2K
NMR and Mass Spectroscopy of Carboxylic Acids01:30

NMR and Mass Spectroscopy of Carboxylic Acids

5.3K
In ¹H NMR spectroscopy, acidic protons (–COOH) of carboxylic acids are highly deshielded and absorb far downfield, at around 9–12 ppm. The chemical shift value depends on the concentration and solvent used.
While α protons of carboxylic acids absorb at 2–2.5 ppm, β protons absorb further upfield.
Carboxylic acids are easily identified by dissolving them in deuterium oxide, which results in a rapid exchange of the acidic protons with deuterium. This leads to the...
5.3K

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Nonuniform Sampling for NMR Spectroscopy.

Scott Robson1, Haribabu Arthanari2, Sven G Hyberts1

  • 1Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, United States.

Methods in Enzymology
|January 7, 2019
PubMed
Summary
This summary is machine-generated.

Nonuniform sampling (NUS) enhances Nuclear Magnetic Resonance (NMR) data acquisition, improving spectrum resolution and reducing measurement time. This technique is crucial for high-resolution 3D and 4D protein NMR spectra.

Keywords:
DFTData reconstructionFFTNMRNonuniform samplingResolutionSensitivitySparse sampling

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Area of Science:

  • Nuclear Magnetic Resonance (NMR) Spectroscopy
  • Biophysical Chemistry
  • Structural Biology

Background:

  • Nonuniform sampling (NUS) offers an alternative to traditional sampling methods for multidimensional NMR data.
  • Initial adoption was limited, but significant gains in measurement time and spectrum resolution have driven wider acceptance.
  • Advancements in NMR software and processing tools have enabled high-quality reconstructions of NUS data.

Purpose of the Study:

  • To review the principles and applications of nonuniform sampling (NUS) in NMR spectroscopy.
  • To highlight the advantages of NUS for acquiring high-resolution multidimensional NMR spectra.
  • To discuss the suitability of NUS for various types of NMR experiments, including those with sparse or crowded spectra.

Main Methods:

  • Exploration of NUS principles and its application in various NMR experiments.
  • Comparison of NUS with uniform sampling for data acquisition.
  • Discussion of processing tools for reconstructing NUS data.
  • Analysis of optimal sampling schedules for different spectral characteristics.

Main Results:

  • NUS significantly improves measurement time and spectrum resolution, particularly for high-resolution 3D and 4D protein NMR.
  • NUS is optimal for sparse, low dynamic-range NMR spectra, such as triple resonance experiments.
  • NUS can aid in detecting weak peaks in high dynamic-range spectra and is feasible for 2D HSQC-like spectra.
  • NUS is a promising approach for high dynamic-range spectra if spectral crowding is reduced.

Conclusions:

  • Nonuniform sampling (NUS) is a powerful technique for advancing NMR spectroscopy, enabling higher resolution and efficiency.
  • NUS is particularly beneficial for complex protein NMR studies and offers solutions for spectral crowding.
  • Continued development and application of NUS promise further breakthroughs in structural biology and chemical analysis.