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Related Concept Videos

NMR Spectroscopy Of Amines01:19

NMR Spectroscopy Of Amines

11.1K
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

6.3K
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

11.2K
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...
11.2K
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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Assessment of Cardiac Function and Energetics in Isolated Mouse Hearts Using 31P NMR Spectroscopy
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XLSY: Extra-Large NMR Spectroscopy.

Yulia Pustovalova1, Maxim Mayzel2, Vladislav Yu Orekhov1,2

  • 1Department of Chemistry and Molecular Biology, University of Gothenburg, P.O. Box 465, Gothenburg, 405 30, Sweden.

Angewandte Chemie (International Ed. in English)
|September 4, 2018
PubMed
Summary
This summary is machine-generated.

Extra-large NMR spectroscopy (XLSY) enables high-resolution, multi-dimensional data for complex biomolecules. This new method reconstructs challenging seven-dimensional spectra, advancing NMR capabilities for intrinsically disordered proteins.

Keywords:
NMR spectroscopyXLSYintrinsically disordered proteinnon-uniform sampling

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Area of Science:

  • Biophysics
  • Structural Biology
  • Nuclear Magnetic Resonance (NMR) Spectroscopy

Background:

  • High-resolution and high-dimensionality NMR spectra are crucial for studying complex biomolecular systems, particularly intrinsically disordered proteins.
  • Existing NMR techniques face limitations in spectral resolution and dimensionality for such challenging systems.

Purpose of the Study:

  • To present an efficient approach, extra-large NMR spectroscopy (XLSY), for collecting, reconstructing, and handling very large NMR spectra.
  • To demonstrate the capability of XLSY in acquiring high-quality, high-dimensional NMR data for intrinsically disordered proteins.

Main Methods:

  • Combination of radial and non-uniform sampling strategies for efficient data acquisition.
  • Development of a novel processing algorithm tailored for large NMR spectra reconstruction.
  • Rigorous statistical validation to ensure the accuracy and reliability of the reconstructed data.
  • Application of XLSY to collect seven-dimensional HNCOCACONH and five-dimensional HACACONH and HN(CA)CONH spectra.

Main Results:

  • Successful high-quality reconstruction of a full seven-dimensional HNCOCACONH spectrum.
  • Demonstration of high-quality reconstruction for two five-dimensional spectra: HACACONH and HN(CA)CONH.
  • Acquisition of complex multidimensional NMR data for α-synuclein, a representative intrinsically disordered protein.

Conclusions:

  • Extra-large NMR spectroscopy (XLSY) is a powerful and efficient method for obtaining high-resolution, high-dimensional NMR spectra.
  • XLSY significantly enhances the NMR toolbox for challenging biomolecular studies, especially for intrinsically disordered proteins.
  • The presented approach overcomes previous limitations in spectral dimensionality and data handling for complex systems.