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Related Concept Videos

¹H NMR of Labile Protons: Deuterium (²H) Substitution00:48

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

1.1K
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.
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¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)01:20

¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)

1.3K
When proton-coupled carbon-13 spectra are simplified by a broadband proton decoupling technique, structural information about the coupled protons is lost. Distortionless enhancement by polarization transfer (DEPT) is a technique that provides information on the number of hydrogens attached to each carbon in a molecule. While the DEPT experiment utilizes complex pulse sequences, the pulse delay and flip angle are specifically manipulated. The resulting signals have different phases depending on...
1.3K
Nuclear Overhauser Enhancement (NOE)01:07

Nuclear Overhauser Enhancement (NOE)

1.0K
Irradiation of a spin-active nucleus causes an increase or decrease in the signal intensity of neighboring nuclei that are not necessarily chemically bonded or involved in J-coupling.  This phenomenon, called the Nuclear Overhauser Enhancement (NOE), results from through-space interactions between the nuclear spins. The NOE effect decreases with increasing internuclear distance and is generally not observed beyond 4 angstroms. In NOE, dipole-dipole interactions between neighboring...
1.0K
¹³C NMR: ¹H–¹³C Decoupling01:04

¹³C NMR: ¹H–¹³C Decoupling

1.3K
The probability of having two carbon-13 atoms next to each other is negligible because of the low natural abundance of carbon-13. Consequently, peak splitting due to carbon-carbon spin-spin coupling is not observed in spectra. However, protons up to three sigma bonds away split the carbon signal according to the n+1 rule, resulting in complicated spectra.
A broadband decoupling technique is used to simplify these complex, sometimes overlapping, signals. Broadband decoupling relies on a...
1.3K
Double Resonance Techniques: Overview01:12

Double Resonance Techniques: Overview

438
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...
438
Atomic Nuclei: Nuclear Spin State Population Distribution01:14

Atomic Nuclei: Nuclear Spin State Population Distribution

1.5K
Near absolute zero temperatures, in the presence of a magnetic field, the majority of nuclei prefer the lower energy spin-up state to the higher energy spin-down state. As temperatures increase, the energy from thermal collisions distributes the spins more equally between the two states. The Boltzmann distribution equation gives the ratio of the number of spins predicted in the spin −½ (N−) and spin +½ (N+) states.
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Related Experiment Video

Updated: Nov 6, 2025

Neutron Crystallography Data Collection and Processing for Modelling Hydrogen Atoms in Protein Structures
10:10

Neutron Crystallography Data Collection and Processing for Modelling Hydrogen Atoms in Protein Structures

Published on: December 1, 2020

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Deuteration Aiming for Neutron Scattering.

Aya Okuda1, Rintaro Inoue1, Ken Morishima1

  • 1Institute for Integrated Radiation and Nuclear Science, Kyoto University, Sennan-gun, Osaka 590-0494 Japan.

Biophysics and Physicobiology
|May 6, 2021
PubMed
Summary

Neutron scattering visualizes proteins using hydrogen and deuterium differences. This study presents a protocol to overcome challenges in protein deuteration for broader neutron scattering applications.

Keywords:
contrast matching methodneutron scatteringprotein deuteration

More Related Videos

Studying Soft-matter and Biological Systems over a Wide Length-scale from Nanometer and Micrometer Sizes at the Small-angle Neutron Diffractometer KWS-2
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Studying Soft-matter and Biological Systems over a Wide Length-scale from Nanometer and Micrometer Sizes at the Small-angle Neutron Diffractometer KWS-2

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High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
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High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

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Related Experiment Videos

Last Updated: Nov 6, 2025

Neutron Crystallography Data Collection and Processing for Modelling Hydrogen Atoms in Protein Structures
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Studying Soft-matter and Biological Systems over a Wide Length-scale from Nanometer and Micrometer Sizes at the Small-angle Neutron Diffractometer KWS-2
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Studying Soft-matter and Biological Systems over a Wide Length-scale from Nanometer and Micrometer Sizes at the Small-angle Neutron Diffractometer KWS-2

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High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
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High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

Published on: April 28, 2022

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Area of Science:

  • Biophysics
  • Structural Biology
  • Biochemistry

Background:

  • Neutron scattering is a powerful technique for visualizing biological molecules.
  • The isotope effect, specifically the difference in neutron scattering between hydrogen and deuterium, allows for selective contrast of molecules.
  • Deuterated proteins enable selective visualization of target proteins within complex systems.

Purpose of the Study:

  • To present a protocol for protein deuteration techniques.
  • To address the challenges of difficulty, high cost, and deuteration ratio control in protein deuteration for neutron scattering.

Main Methods:

  • Development and optimization of a comprehensive protein deuteration protocol.
  • Methods for controlling and determining the deuteration ratio of protein samples.

Main Results:

  • A standardized protocol for efficient and cost-effective protein deuteration.
  • Reliable methods for assessing and controlling the level of deuteration.

Conclusions:

  • The presented protocol facilitates wider adoption of neutron scattering studies involving deuterated proteins.
  • This work aims to lower the barrier to entry for researchers utilizing neutron scattering for complex biological systems.