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Related Concept Videos

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...
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...
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 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...
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.

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Related Experiment Video

Updated: Jun 1, 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

Backbone resonance assignment and order tensor estimation using residual dipolar couplings.

Paul Shealy1, Yizhou Liu, Mikhail Simin

  • 1Department of Computer Science and Engineering, University of South Carolina, Columbia, SC 29208, USA.

Journal of Biomolecular NMR
|June 14, 2011
PubMed
Summary
This summary is machine-generated.

A new method, Exhaustively Permuted Assignment of RDCs (EPAR), rapidly assigns nuclear magnetic resonance (NMR) data to protein structures. This cost-effective approach uses residual dipolar couplings (RDCs) and existing structural information, improving efficiency in structural biology research.

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Förster Resonance Energy Transfer Mapping: A New Methodology to Elucidate Global Structural Features

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Last Updated: Jun 1, 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

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

F&#246;rster Resonance Energy Transfer Mapping: A New Methodology to Elucidate Global Structural Features
07:09

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Area of Science:

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

Background:

  • Nuclear magnetic resonance (NMR) studies of proteins with known X-ray structures are valuable.
  • Traditional NMR resonance assignment is costly and often ignores existing structural data, requiring uniform isotope labeling.

Purpose of the Study:

  • To develop a rapid and cost-effective method for assigning NMR data to known protein structures (X-ray or modeled).
  • To leverage unassigned residual dipolar coupling (RDC) data for efficient structure-based NMR assignment.

Main Methods:

  • The Exhaustively Permuted Assignment of RDCs (EPAR) algorithm was developed.
  • EPAR utilizes backbone N-H RDCs from multiple alignment media and amino acid type information.
  • The method builds upon previous work, incorporating several extensions.

Main Results:

  • EPAR achieved >80% average assignment accuracy with two alignment media and >94% with three.
  • The algorithm was validated on 13 synthetic and experimental datasets from 8 diverse protein structures.
  • EPAR provides a reliable prediction of assignment accuracy, correlated with true accuracy (0.77).

Conclusions:

  • EPAR offers a significant improvement in speed and cost-effectiveness for NMR resonance assignment.
  • The method effectively integrates existing structural information with RDC data.
  • EPAR's accuracy and predictive capability enhance confidence in structural biology investigations.