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Related Concept Videos

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...
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...
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...
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...
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...
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.

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Related Experiment Video

Updated: May 13, 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

Biomolecular magic-angle spinning solid-state NMR: recent methods and applications.

Amir Goldbourt1

  • 1School of Chemistry, Raymond and Beverly Sackler Faculty of Exact Sciences, Tel Aviv University, Tel Aviv 69978, Israel. amirgo@post.tau.ac.il

Current Opinion in Biotechnology
|March 14, 2013
PubMed
Summary
This summary is machine-generated.

Magic-angle spinning solid-state NMR (MAS SSNMR) reveals the structure and dynamics of complex biomolecules. This technique is crucial for studying insoluble and non-crystalline biological systems.

More Related Videos

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

Related Experiment Videos

Last Updated: May 13, 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:

  • Biophysics
  • Structural Biology
  • Biochemistry

Background:

  • Understanding biomolecular structure-dynamics-function relationships is key to cellular processes.
  • Biophysical techniques are essential for characterizing complex biological systems.
  • Magic-angle spinning solid-state NMR (MAS SSNMR) offers unique insights into biomolecular structures.

Purpose of the Study:

  • To review recent advancements in characterizing macromolecular assemblies using MAS SSNMR.
  • To highlight the utility of MAS SSNMR for studying challenging biomolecular systems.

Main Methods:

  • Magic-angle spinning solid-state nuclear magnetic resonance (MAS SSNMR) spectroscopy.
  • Characterization of macromolecular assemblies, viruses, membrane proteins, amyloid fibrils, and protein aggregates.

Main Results:

  • MAS SSNMR provides detailed structural information on biomolecules.
  • The technique is particularly valuable for non-soluble, large molecular-weight, and non-crystalline biomolecules.
  • Recent progress has expanded the application of MAS SSNMR to diverse biological systems.

Conclusions:

  • MAS SSNMR is a powerful tool for elucidating the structure and dynamics of complex biomolecules.
  • This technique is indispensable for studying systems intractable by other methods.
  • Continued advancements in MAS SSNMR will further enhance our understanding of biological functions.