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Related Concept Videos

2D NMR: Overview of Heteronuclear Correlation Techniques01:18

2D NMR: Overview of Heteronuclear Correlation Techniques

284
Heteronuclear correlation spectroscopy is an analytical technique that investigates the coupling between different types of nuclei, often a proton and an X-nucleus, such as carbon-13 or nitrogen-15. This method is commonly used in nuclear magnetic resonance (NMR) spectroscopy to gain insights into complex chemical compounds' structural and compositional aspects. A typical heteronuclear correlation spectrum displays X-nucleus chemical shifts on one axis and a proton spectrum on the other...
284
2D NMR: Overview of Homonuclear Correlation Techniques01:16

2D NMR: Overview of Homonuclear Correlation Techniques

275
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...
275
2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)01:19

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

866
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...
866
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.
4.9K
NMR Spectrometers: Overview01:20

NMR Spectrometers: Overview

1.3K
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...
1.3K
Applications Of NMR In Biology01:25

Applications Of NMR In Biology

3.8K
Nuclear magnetic resonance (NMR) spectroscopy is a very valuable analytical technique for researchers. It has been used for more than 50 years as an analytical tool. F. Bloch and E. Purcell formulated NMR in 1946 and won the 1952 Nobel Prize in Physics  for their work. Biological macromolecules such as proteins, nucleic acids, lipids, and organic molecules including pharmaceutical compounds, can be studied using this versatile tool that exploits the magnetic properties of certain nuclei.
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Related Experiment Video

Updated: Aug 30, 2025

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

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GPCR structural characterization by NMR spectroscopy in solution.

Lingyun Yang1, Dongsheng Liu1, Kurt Wüthrich1,2,3

  • 1iHuman Institute, ShanghaiTech University, Shanghai 201210, China.

Acta Biochimica Et Biophysica Sinica
|August 26, 2022
PubMed
Summary
This summary is machine-generated.

Nuclear Magnetic Resonance (NMR) spectroscopy reveals G-protein-coupled receptor (GPCR) dynamics and interactions. These insights enhance understanding of GPCRs for improved drug design.

Keywords:
G protein-coupled receptor dynamicsGPCR biologydrug developmentfluorine-19 NMRstable-isotope labeling

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Pharmacology

Background:

  • G-protein-coupled receptors (GPCRs) are crucial cell surface proteins involved in signal transduction.
  • Understanding GPCR dynamics and interactions is vital for drug discovery and development.

Approach:

  • This review explores various Nuclear Magnetic Resonance (NMR) spectroscopy techniques.
  • Methods discussed include stable-isotope labeling, site-specific genetic engineering, 19F-NMR probes, and spin labeling.

Key Points:

  • NMR spectroscopy provides insights into GPCR conformational dynamics at physiological temperatures.
  • It elucidates intermolecular interactions crucial for GPCR function.
  • Various labeling strategies enable detailed structural and dynamic analysis.

Conclusions:

  • NMR spectroscopy complements structural methods like X-ray crystallography and cryo-EM.
  • It offers unique data on GPCR dynamics and interactions.
  • This knowledge advances GPCR biology and supports rational drug design.