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Related Concept Videos

¹³C NMR: ¹H–¹³C Decoupling01:04

¹³C NMR: ¹H–¹³C Decoupling

The probability of having two carbon-13 atoms next to each other is negligible because of the low natural abundance of carbon-13. Consequently, peak splitting due to carbon-carbon spin-spin coupling is not observed in spectra. However, protons up to three sigma bonds away split the carbon signal according to the n+1 rule, resulting in complicated spectra.
A broadband decoupling technique is used to simplify these complex, sometimes overlapping, signals. Broadband decoupling relies on a...
Double Resonance Techniques: Overview01:12

Double Resonance Techniques: Overview

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...
2D NMR: Overview of Heteronuclear Correlation Techniques01:18

2D NMR: Overview of Heteronuclear Correlation Techniques

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 axis.
2D NMR: Overview of Homonuclear Correlation Techniques01:16

2D NMR: Overview of Homonuclear Correlation Techniques

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

NMR Spectroscopy: Spin–Spin Coupling

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 in...
¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

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 slanted or...

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NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
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Published on: November 1, 2024

Broadband Heteronuclear Solid-State NMR Experiments by Exponentially Modulated Dipolar Recoupling without Decoupling.

Anders B Nielsen1, Lasse A Straasø, Andrew J Nieuwkoop

  • 1Center for Insoluble Protein Structures (inSPIN), Interdiscipolinary Nanoscience Center (iNANO) and Department of Chemistry, Aarhus University, DK-8000 Aarhus C, Denmark.

The Journal of Physical Chemistry Letters
|August 7, 2010
PubMed
Summary

We developed a new solid-state NMR technique, EXPonentially mOdulated Recoupling Technique (EXPORT), for efficient heteronuclear dipolar recoupling. This method avoids sample heating caused by high-power proton decoupling, enhancing sample integrity.

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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Last Updated: Jun 10, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
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Published on: November 1, 2024

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

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

Published on: September 17, 2017

Area of Science:

  • Solid-state Nuclear Magnetic Resonance (NMR) spectroscopy
  • Advanced spectroscopic techniques
  • Biophysical chemistry

Background:

  • Heteronuclear dipolar recoupling is crucial for structure determination in solid-state NMR.
  • Existing methods often require high-power proton decoupling, leading to sample heating and potential degradation.
  • There is a need for efficient recoupling techniques that minimize sample heating.

Purpose of the Study:

  • To introduce a novel solid-state NMR method for heteronuclear dipolar recoupling without proton decoupling.
  • To demonstrate the efficiency and flexibility of the new technique for various applications.
  • To address the issue of sample heating associated with traditional methods.

Main Methods:

  • Development of the EXPonentially mOdulated Recoupling Technique (EXPORT) using exponentially modulated radiofrequency fields.
  • Analytical and numerical description of the EXPORT method.
  • Experimental validation using 1D (13)C and 2D (13)C-(15)N correlation NMR spectroscopy.

Main Results:

  • EXPORT provides efficient broadband heteronuclear dipolar recoupling.
  • The method operates without high-power proton decoupling, mitigating sample heating.
  • Successful application to (13)C,(15)N-labeled proteins (GB1, ubiquitin) and amyloidogenic peptides (SNNFGAILSS fragment).

Conclusions:

  • EXPORT is a flexible, robust, and high-performing technique for solid-state NMR.
  • It offers significant advantages over existing methods by avoiding sample heating.
  • The technique is expected to be widely adopted for both hetero- and homonuclear recoupling in diverse chemical and biological applications.