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Related Concept Videos

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...
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.
2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)01:19

2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)

Heteronuclear single-quantum correlation spectroscopy (HSQC) is a 2D NMR technique that reveals one-bond correlations between hydrogen and a heteronucleus. The HSQC experiment is similar to the heteronuclear correlation experiment (HETCOR) but is more sensitive. In the HSQC spectrum, the proton chemical shift is plotted on the horizontal F2 axis, while the 13C chemical shift is plotted on the vertical F1 axis. The corresponding proton and 13C spectra are also shown. The HSQC contour plot does...
¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR01:15

¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR

The axial and equatorial protons in cyclohexane can be distinguished by performing a variable-temperature NMR experiment. In this process, except for one proton, the remaining eleven protons are replaced by deuterium. The deuterium substitution avoids the possible peak splitting caused by the spin-spin coupling between the adjacent protons. The remaining proton flips between the axial and equatorial positions.
¹H NMR of Labile Protons: Deuterium (²H) Substitution00:48

¹H NMR of Labile Protons: Deuterium (²H) Substitution

This lesson illustrates the role of deuterium substitution in simplifying the NMR spectrum of compounds comprising labile protons. One method employed is the use of deuterium. Amongst the three isotopes of hydrogen, deuterium (2H) has a nucleus composed of one proton and one neutron. When the D2O solvent is added to a pure dry ethanol solution, its labile proton is substituted with deuterium.
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 24, 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

4D solid-state NMR for protein structure determination.

Matthias Huber1, Anja Böckmann, Sebastian Hiller

  • 1Physical Chemistry, ETH Zurich, Wolfgang-Pauli-Strasse 10, 8093 Zürich, Switzerland.

Physical Chemistry Chemical Physics : PCCP
|March 10, 2012
PubMed
Summary
This summary is machine-generated.

Higher-dimensional solid-state NMR experiments, like 4D proton-detected spectra, improve structural studies of challenging proteins. These advanced techniques provide more distance restraints for atomic-resolution protein structure determination.

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15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the &#181;s-ms Timescale
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15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale

Published on: April 19, 2021

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Last Updated: May 24, 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

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the &#181;s-ms Timescale
08:09

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale

Published on: April 19, 2021

Area of Science:

  • Biophysical Chemistry
  • Structural Biology
  • Nuclear Magnetic Resonance Spectroscopy

Background:

  • Solid-state NMR enables structural studies of proteins intractable by other methods, including fibrils and membrane proteins.
  • Traditional 2D NMR spectra often face severe resonance overlap, limiting detailed structural analysis.
  • Atomic-resolution structural data is crucial for understanding protein function and disease mechanisms.

Purpose of the Study:

  • To explore the potential of higher-dimensional (3D and 4D) proton-detected solid-state NMR experiments.
  • To address the challenge of resonance overlap in 2D NMR spectra of proteins.
  • To enhance the identification and assignment of distance restraints for protein structure determination.

Main Methods:

  • Analysis of higher-dimensional (3D and 4D) proton-detected solid-state NMR experiments.
  • Discussion of practical considerations for NMR measurements and protein sample preparation.
  • Structure calculations utilizing data from 4D solid-state NMR spectra.

Main Results:

  • Higher-dimensional NMR experiments significantly increase the number of identifiable and assignable distance restraints.
  • 4D solid-state NMR spectra yield valuable data for protein structure calculations.
  • The study demonstrates the feasibility and advantages of advanced NMR techniques for structural biology.

Conclusions:

  • Higher-dimensional solid-state NMR is a powerful approach for atomic-resolution structural studies of challenging proteins.
  • These advanced NMR techniques overcome limitations of 2D spectra, enabling more comprehensive structural insights.
  • The findings support the broader application of 3D and 4D NMR in structural biology research.