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Related Concept Videos

NMR Spectroscopy Of Amines01:19

NMR Spectroscopy Of Amines

11.0K
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...
11.0K
NMR Spectroscopy of Aromatic Compounds01:14

NMR Spectroscopy of Aromatic Compounds

6.2K
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.
6.2K
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

3.1K
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...
3.1K
NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

3.0K
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...
3.0K
NMR and Mass Spectroscopy of Carboxylic Acids01:30

NMR and Mass Spectroscopy of Carboxylic Acids

5.2K
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...
5.2K

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Preparation of Fungal and Plant Materials for Structural Elucidation Using Dynamic Nuclear Polarization Solid-State NMR
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Preparation of Fungal and Plant Materials for Structural Elucidation Using Dynamic Nuclear Polarization Solid-State NMR

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High-sensitivity protein solid-state NMR spectroscopy.

Venkata S Mandala1, Mei Hong1

  • 1Department of Chemistry, Massachusetts Institute of Technology, 170 Albany Street, Cambridge, MA 02139, United States.

Current Opinion in Structural Biology
|April 30, 2019
PubMed
Summary
This summary is machine-generated.

Solid-state nuclear magnetic resonance (SSNMR) spectroscopy sensitivity is enhanced by 1H detection with fast magic-angle spinning (MAS) and dynamic nuclear polarization (DNP). These techniques enable detailed studies of proteins and large biomolecular complexes.

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Area of Science:

  • Structural biology
  • Biophysics
  • Spectroscopy

Background:

  • Solid-state nuclear magnetic resonance (SSNMR) spectroscopy is crucial for understanding biomolecular structures.
  • Enhancing SSNMR sensitivity is key to studying challenging biological systems.
  • Current limitations hinder the analysis of low-abundance or complex biomolecules.

Purpose of the Study:

  • To highlight advancements in SSNMR sensitivity for structural biology.
  • To showcase the applications of 1H detection with fast magic-angle spinning (MAS) and dynamic nuclear polarization (DNP).
  • To identify future research directions in SSNMR technology.

Main Methods:

  • Utilizing 1H detection under fast magic-angle spinning (MAS) for enhanced sensitivity.
  • Employing dynamic nuclear polarization (DNP) to transfer polarization from electron spins to nuclear spins.
  • Applying these techniques to study protein structure, dynamics, and interactions.

Main Results:

  • 1H detection with fast MAS significantly improves the study of small protein quantities under physiological conditions.
  • DNP enables the investigation of large biomolecular complexes, protein intermediates, and conformational distributions in lipid membranes and cells.
  • Recent applications demonstrate the power of these emerging SSNMR technologies.

Conclusions:

  • Advanced SSNMR techniques, including fast MAS and DNP, offer unprecedented sensitivity for structural biology.
  • These methods expand the scope of SSNMR to address complex biological questions.
  • Further development holds promise for even greater insights into biomolecular mechanisms.