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Related Concept Videos

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...
Applications Of NMR In Biology01:25

Applications Of NMR In Biology

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.
The...
Spin–Spin Coupling Constant: Overview01:08

Spin–Spin Coupling Constant: Overview

In bromoethane, the three methyl protons are coupled to the two methylene protons that are three bonds away. In accordance with the n+1 rule, the signal from the methyl protons is split into three peaks with 1:2:1 relative intensities. The methylene protons appear as a quartet, with the relative intensities of 1:3:3:1.
Qualitatively, any spin plus-half nucleus polarizes the spins of its electrons to the minus-half state. Consequently, the paired electron in the hydrogen–carbon bond must have a...
Spin–Spin Coupling: Two-Bond Coupling (Geminal Coupling)01:20

Spin–Spin Coupling: Two-Bond Coupling (Geminal Coupling)

Two NMR-active nuclei bonded to a central atom can be involved in geminal or two-bond coupling. Geminal coupling is commonly seen between diastereotopic protons in chiral molecules and unsymmetrical alkenes, among others.
The central atom need not be NMR-active because its electrons are affected by the electron polarization of the spin-active atoms. However, spin information is transmitted less effectively than in one-bond coupling, and 2J values are usually weaker than 1J values. The energy of...
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...

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Updated: May 20, 2026

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

Magic angle spinning solid-state NMR experiments for structural characterization of proteins.

Lichi Shi1, Vladimir Ladizhansky

  • 1Department of Physics and Biophysical Interdepartmental Group, University of Guelph, Guelph, ON, Canada.

Methods in Molecular Biology (Clifton, N.J.)
|July 5, 2012
PubMed
Summary

This study details protocols for 3D magic angle spinning (MAS) solid-state nuclear magnetic resonance (SSNMR) experiments, crucial for assigning chemical shifts in large, insoluble proteins and biomolecular complexes.

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

Published on: October 9, 2020

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Last Updated: May 20, 2026

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

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

Area of Science:

  • Biophysics
  • Structural Biology
  • Biochemistry

Background:

  • Solid-state nuclear magnetic resonance (SSNMR) is vital for characterizing insoluble biological macromolecules.
  • Obtaining spectroscopic assignments (chemical shifts) is critical but challenging for large proteins due to decreased sensitivity and resolution.

Purpose of the Study:

  • To describe a standard protocol for 3D magic angle spinning (MAS) SSNMR experiments.
  • To provide guidance for researchers applying SSNMR to large proteins and aggregates.

Main Methods:

  • Detailed protocol for common 3D MAS SSNMR experiments.
  • Focus on techniques applicable to insoluble proteins and protein aggregates.

Main Results:

  • Established procedures for SSNMR spectroscopic assignments are presented.
  • The protocol aims to enhance the application of SSNMR for larger biomolecular systems.

Conclusions:

  • The described 3D MAS SSNMR protocols offer a valuable resource for structural characterization of challenging biomolecules.
  • This work facilitates the extension of SSNMR techniques to a broader range of biological systems.