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Related Concept Videos

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...
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...
¹H NMR: Long-Range Coupling01:27

¹H NMR: Long-Range Coupling

The coupling interactions of nuclei across four or more bonds are usually weak, with J values less than 1 Hz. While these are usually not observed in spectra, the presence of multiple bonds along the coupling pathway can result in observable long-range coupling.
In alkenes, spin information is communicated via σ–π overlap, as seen in allylic (four-bond) and homoallylic (five-bond) couplings. These coupling interactions are stronger when the σ bond is parallel to the alkene π orbitals.
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...
NMR Spectrometers: Resolution and Error Correction01:14

NMR Spectrometers: Resolution and Error Correction

When magnetic nuclei in a sample achieve resonance and undergo relaxation, the signal detected in NMR is an approximately exponential free induction decay. Fourier transform of an exponential decay yields a Lorentzian peak in the frequency domain. Lorentzian peaks in an NMR spectrum are defined by their amplitude, full width at half maximum, and position, where the peak width is governed by the spin-spin relaxation time alone. In real experiments, however, the applied magnetic field is rendered...
Two-Dimensional (2D) NMR: Overview01:12

Two-Dimensional (2D) NMR: Overview

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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Related Experiment Video

Updated: Jun 5, 2026

High-Temperature and High-Pressure In situ Magic Angle Spinning Nuclear Magnetic Resonance Spectroscopy
08:55

High-Temperature and High-Pressure In situ Magic Angle Spinning Nuclear Magnetic Resonance Spectroscopy

Published on: October 9, 2020

Longer-range distances by spinning-angle-encoding solid-state NMR spectroscopy.

Johanna Becker-Baldus1, Thomas F Kemp, Jaan Past

  • 1Department of Physics, University of Warwick, Coventry, UK CV4 7AL.

Physical Chemistry Chemical Physics : PCCP
|January 25, 2011
PubMed
Summary
This summary is machine-generated.

Researchers developed a new solid-state NMR method to measure long-range carbon-carbon distances in peptides. This technique enhances sensitivity and resolution for accurate molecular structure determination.

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

Published on: September 17, 2017

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Last Updated: Jun 5, 2026

High-Temperature and High-Pressure In situ Magic Angle Spinning Nuclear Magnetic Resonance Spectroscopy
08:55

High-Temperature and High-Pressure In situ Magic Angle Spinning Nuclear Magnetic Resonance Spectroscopy

Published on: October 9, 2020

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
  • Biophysical Chemistry
  • Structural Biology

Background:

  • Determining long-range distances in biomolecules is crucial for understanding their structure and function.
  • Traditional NMR methods often face limitations in sensitivity and resolution for such measurements.

Purpose of the Study:

  • To develop and validate a novel solid-state NMR approach for accurate determination of C-C distances exceeding 4 Å.
  • To enhance sensitivity and resolution in solid-state NMR experiments for structural analysis of labeled peptides.

Main Methods:

  • Utilized a spinning-angle-encoding spin-echo solid-state NMR technique.
  • Recorded dipolar coupling-dependent spin-echo modulation off-magic angle and acquired free-induction decay at the magic angle.
  • Redesigned a 600 MHz HX MAS NMR probe for fast angle switching (up to ~5° in ~10 ms at 12 kHz MAS for 1.8 mm rotors).
  • Implemented a combined reference and dipolar-modulated experiment with a master-curve approach for data interpretation.

Main Results:

  • Successfully determined a C-C distance over 4 Å in a fully labeled dipeptide with high accuracy.
  • Achieved optimal sensitivity by strategically switching between off-magic and magic angles.
  • Retained both ideal resolution and long-range distance sensitivity through probe redesign and fast angle switching.

Conclusions:

  • The new spinning-angle-encoding spin-echo solid-state NMR approach provides a robust method for measuring long-range C-C distances.
  • This technique offers significant improvements in sensitivity and resolution, advancing structural studies of peptides and other biomolecules.
  • The redesigned NMR probe and data interpretation strategy enable precise structural insights previously inaccessible.