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Related Concept Videos

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

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

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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.
946
Hydrogen Bonds00:26

Hydrogen Bonds

121.8K
Hydrogen bonds are weak attractions between atoms that have formed other chemical bonds. One of these atoms is electronegative, like oxygen, and has a partial negative charge. The other is a hydrogen atom that has bonded with another electronegative atom and has a partial positive charge.
Hydrogen Bonds Control the World!
Because hydrogen has very weak electronegativity when it binds with a strongly electronegative atom, such as oxygen or nitrogen, electrons in the bond are unequally shared....
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Double Resonance Techniques: Overview01:12

Double Resonance Techniques: Overview

260
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...
260
¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)01:20

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

1.1K
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...
1.1K
2D NMR: Overview of Heteronuclear Correlation Techniques01:18

2D NMR: Overview of Heteronuclear Correlation Techniques

265
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...
265
Reduction of Alkenes: Catalytic Hydrogenation02:13

Reduction of Alkenes: Catalytic Hydrogenation

12.3K
Alkenes undergo reduction by the addition of molecular hydrogen to give alkanes. Because the process generally occurs in the presence of a transition-metal catalyst, the reaction is called catalytic hydrogenation.
Metals like palladium, platinum, and nickel are commonly used in their solid forms — fine powder on an inert surface. As these catalysts remain insoluble in the reaction mixture, they are referred to as heterogeneous catalysts.
The hydrogenation process takes place on the...
12.3K

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Related Experiment Video

Updated: Aug 14, 2025

A Hydrogen-Deuterium Exchange Mass Spectrometry HDX-MS Platform for Investigating Peptide Biosynthetic Enzymes
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A Hydrogen-Deuterium Exchange Mass Spectrometry HDX-MS Platform for Investigating Peptide Biosynthetic Enzymes

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Developments in rapid hydrogen-deuterium exchange methods.

Vimanda Chow1, Esther Wolf1, Cristina Lento1

  • 1Department of Chemistry, York University, Toronto, ON M3J 1P3, Canada.

Essays in Biochemistry
|January 13, 2023
PubMed
Summary

Millisecond timescale hydrogen-deuterium exchange mass spectrometry (HDX-MS) offers unique insights into biomolecular dynamics. This rapid HDX-MS approach reveals details about intrinsically disordered proteins and fast binding interactions, crucial for understanding diseases.

Keywords:
conformational dynamicshydrogen-deuterium exchange mass spectrometryintrinsically disordered proteinsmass spectrometryprotein structure

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Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions
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Area of Science:

  • Biochemistry
  • Biophysics
  • Analytical Chemistry

Background:

  • Biological macromolecules feature exchangeable hydrogens crucial for structure and dynamics.
  • Hydrogen-deuterium exchange mass spectrometry (HDX-MS) leverages this exchange to study biomolecular properties.
  • Conventional HDX-MS operates on second-to-hour timescales, limiting insights into faster processes.

Purpose of the Study:

  • To review millisecond timescale HDX-MS techniques and applications.
  • To highlight the advantages of rapid HDX-MS for studying dynamic biomolecular events.
  • To emphasize the importance of extending HDX-MS timescales for broader biological insights.

Main Methods:

  • Focus on millisecond timescale hydrogen-deuterium exchange mass spectrometry (HDX-MS).
  • Review technical advancements enabling rapid HDX measurements.
  • Analyze applications across proteins, nucleic acids, and carbohydrates.

Main Results:

  • Millisecond HDX-MS provides unique data on weakly structured species and fast binding interactions.
  • This technique is valuable for studying intrinsically disordered proteins/regions (IDPs/IDRs) linked to diseases.
  • Rapid HDX-MS can elucidate nucleic acid and carbohydrate structures, including isomers and loops, and assess rigidity.

Conclusions:

  • Broadening the HDX-MS timescale to milliseconds significantly enhances throughput.
  • Rapid HDX-MS captures a wider spectrum of function-relevant dynamics and structural shifts.
  • This expanded timescale is vital for a comprehensive understanding of biomolecular behavior and disease mechanisms.