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Related Concept Videos

Two-Dimensional (2D) NMR: Overview01:12

Two-Dimensional (2D) NMR: Overview

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The 1D NMR spectrum of large and complex molecules like natural products has complicated splitting patterns and overlapping signals, which can be easily interpreted using 2-dimensional (2D) NMR. Unlike 1D NMR, 2D NMR has two frequency axes that provide the coupling information between the nucleus A and nucleus B in a molecule. The process from which 2D spectra are obtained has four steps.
The first step is the preparation period, during which nucleus A is excited with a radiofrequency pulse....
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¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

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

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

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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...
1.5K
Double Resonance Techniques: Overview01:12

Double Resonance Techniques: Overview

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Double resonance techniques in Nuclear Magnetic Resonance (NMR) spectroscopy involve the simultaneous application of two different frequencies or radiofrequency pulses to manipulate and observe two distinct nuclear spins. One important application of double resonance is spin decoupling, which selectively suppresses coupling with one type of nucleus while observing the NMR signal from another nucleus, simplifying the spectrum and enhancing resolution.
Spin decoupling is usually achieved by...
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¹H NMR: Complex Splitting01:13

¹H NMR: Complex Splitting

2.0K
A proton M that is coupled to a proton X results in doublet signals for M. However, NMR-active nuclei can be simultaneously coupled to more than one nonequivalent nucleus. When M is coupled to a second proton A, such as in styrene oxide, each peak in the doublet is split into another doublet.
Splitting diagrams or splitting tree diagrams are routinely used to depict such complex couplings. While drawing splitting diagrams, the splitting with the larger coupling constant is usually applied...
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Interpreting ¹H NMR Signal Splitting: The (n + 1) Rule01:10

Interpreting ¹H NMR Signal Splitting: The (n + 1) Rule

2.8K
In the AX proton spin system, proton A can sense the two spin states of a coupled proton X, resulting in a doublet NMR signal with two peaks of equal (1:1) intensity. When proton A is coupled to two equivalent protons (AX2 spin system), the spin states of each X can be aligned with or against the external field, creating three possible scenarios. This results in a 1:2:1  triplet signal, where the central peak corresponds to the chemical shift of A and is twice as large or intense as the...
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A New Straightforward Method for Lipophilicity logP Measurement using 19F NMR Spectroscopy
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F 1 F 2-selective NMR spectroscopy.

Erik Walinda1, Daichi Morimoto2, Masahiro Shirakawa2

  • 1Department of Molecular and Cellular Physiology, Graduate School of Medicine, Kyoto University, Sakyo-ku Yoshida Konoe-cho, Kyoto, 606-8501, Japan.

Journal of Biomolecular NMR
|May 6, 2017
PubMed
Summary

A new nuclear magnetic resonance (NMR) method enhances biomolecular studies by selectively sampling signal-rich spectral regions. This approach simplifies data acquisition and analysis for protein and nucleic acid structure and dynamics.

Keywords:
Cross-polarizationDimensional reductionFrequency selectionNuclear overhauser effect spectroscopyRelaxation dispersionSelective excitation

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Area of Science:

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

Background:

  • Fourier transform NMR spectroscopy is crucial for understanding biomolecular structure, interactions, and dynamics.
  • Conventional multidimensional NMR (3D/4D) generates large datasets requiring extensive acquisition time and expert processing.
  • Current methods sample all spectral regions equally, including less informative 'dark' regions, leading to inefficiencies.

Purpose of the Study:

  • To introduce a novel, selective approach for obtaining multidimensional chemical shift correlations in biomolecules.
  • To demonstrate that this method provides equivalent information to conventional 4D NMR experiments but with potential advantages in speed and simplicity.
  • To illustrate the applicability of the selective approach in de novo assignment and structural/dynamics studies.

Main Methods:

  • Development of a new NMR strategy focusing on specific frequency ranges (F1F2) for signal acquisition.
  • Utilizing Hartmann-Hahn cross-polarization with weak radio frequency fields for selective excitation.
  • Acquiring resulting F3F4 correlation spectra using two-dimensional NMR techniques.

Main Results:

  • The selective approach samples only signal-rich ('bright') spectral regions, optimizing data collection.
  • Demonstrated information equivalence to conventional 4D NMR experiments.
  • Successfully applied the method to de novo assignment and studies of ubiquitin and fatty-acid binding protein 4 (FABP4).

Conclusions:

  • The F1F2-selective NMR approach offers a simplified and potentially faster alternative to conventional multidimensional NMR.
  • This method streamlines spectral processing, interpretation, and comparative analysis of biomolecular data.
  • Future extensions could lead to new selective NMR experiments for detailed studies of protein dynamics, interactions, and allosteric modulation.