Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Proton (¹H) NMR: Chemical Shift01:07

Proton (¹H) NMR: Chemical Shift

3.2K
Organic molecules primarily contain carbon and hydrogen atoms. While all the hydrogen isotopes are NMR-active, protium or hydrogen-1 is the most abundant. It has a significant energy separation between its nuclear spin states due to its large gyromagnetic ratio. As per Boltzmann's distribution, an increase in the energy separation implies a greater excess population of nuclei available for excitation, resulting in a strong NMR absorption signal.
Absorption signals of all the protium nuclei...
3.2K
Interpreting ¹H NMR Signal Splitting: The (n + 1) Rule01:10

Interpreting ¹H NMR Signal Splitting: The (n + 1) Rule

2.4K
In the AX proton spin system, proton A can sense the two spin states of a coupled proton X, resulting in a doublet NMR signal with two peaks of equal (1:1) intensity. When proton A is coupled to two equivalent protons (AX2 spin system), the spin states of each X can be aligned with or against the external field, creating three possible scenarios. This results in a 1:2:1  triplet signal, where the central peak corresponds to the chemical shift of A and is twice as large or intense as the...
2.4K
¹H NMR: Complex Splitting01:13

¹H NMR: Complex Splitting

1.8K
A proton M that is coupled to a proton X results in doublet signals for M. However, NMR-active nuclei can be simultaneously coupled to more than one nonequivalent nucleus. When M is coupled to a second proton A, such as in styrene oxide, each peak in the doublet is split into another doublet.
Splitting diagrams or splitting tree diagrams are routinely used to depict such complex couplings. While drawing splitting diagrams, the splitting with the larger coupling constant is usually applied...
1.8K
Other Nuclides: 31P, 19F, 15N NMR01:16

Other Nuclides: 31P, 19F, 15N NMR

737
Many organic, inorganic, and biological molecules contain spin-half nuclei such as nitrogen-15, fluorine-19, and phosphorus-31. As a result, NMR studies of these nuclei have found extensive applications in chemical and biological research.
While fluorine-19 and phosphorous-31 have high natural abundances (100%) and positive gyromagnetic ratios, nitrogen-15 has a low natural abundance and a negative gyromagnetic ratio. However, nitrogen-15 is still preferred over nitrogen-14 (which has a...
737
¹H NMR of Labile Protons: Deuterium (²H) Substitution00:48

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

1.3K
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.
1.3K
¹H NMR Chemical Shift Equivalence: Homotopic and Heterotopic Protons01:03

¹H NMR Chemical Shift Equivalence: Homotopic and Heterotopic Protons

4.1K
Protons in identical electronic environments within a molecule are chemically equivalent and have the same chemical shift. The replacement test is a useful tool to identify chemical equivalence and predict NMR spectra. A substituent replaces each of the protons being examined and the resulting molecules are compared. If the same molecule is obtained, the protons are equivalent or homotopic. Replacement of any hydrogens in ethane by chlorine yields chloroethane because all six protons are...
4.1K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Tuning Connectivity in Hybrid Organic-Inorganic Antimony Halides through Reactant Concentration Effects.

Inorganic chemistry·2026
Same author

Allosteric Regulation of Photophysics and Binding in Oxazine-macrocycle Complexes at Single-molecule Resolution.

Angewandte Chemie (International ed. in English)·2026
Same author

Lipid Pocket Binders Impose Allosteric Changes of Protein Dynamics Around the Active Site of the Protein Kinase p38α.

Angewandte Chemie (International ed. in English)·2026
Same author

High-dimensional solid-state NMR facilitated by transverse-mixing optimal control.

Research square·2025
Same author

Drop Dilution Enables the Use of PEG-Derived Detergents for Membrane Protein Purification.

ACS omega·2025
Same author

Luminescent Chiral Molecular Glasses by Melt-Quenching Enantiopure BINAP.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2025

Related Experiment Video

Updated: Jan 18, 2026

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
09:25

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

Published on: November 1, 2024

2.7K

Protons as Versatile Reporters in Solid-State NMR Spectroscopy.

Suresh K Vasa1,2, Petra Rovó1,2, Rasmus Linser1,2

  • 1Department Chemistry , Ludwig-Maximilians-University Munich , Butenandtstr. 5-13 , 81377 Munich , Germany.

Accounts of Chemical Research
|May 16, 2018
PubMed
Summary

Solid-state nuclear magnetic resonance (ssNMR) now enables high-resolution proton detection, revolutionizing biomolecular characterization. This advancement allows for faster, more accurate analysis of complex molecules and their dynamics.

More Related Videos

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States
04:37

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States

Published on: June 29, 2021

3.1K
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

16.0K

Related Experiment Videos

Last Updated: Jan 18, 2026

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
09:25

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

Published on: November 1, 2024

2.7K
High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States
04:37

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States

Published on: June 29, 2021

3.1K
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

16.0K

Area of Science:

  • Spectroscopic techniques
  • Biophysical chemistry
  • Structural biology

Background:

  • Solid-state nuclear magnetic resonance (ssNMR) with magic-angle spinning (MAS) is crucial for atomic-resolution molecular characterization.
  • Proton (¹H) detection in ssNMR, despite its high natural abundance and gyromagnetic ratio, has historically faced challenges.
  • Previous limitations included detrimental effects from the high gyromagnetic ratio and the need for expensive sample deuteration.

Purpose of the Study:

  • To describe the fundamentals of proton detection in ssNMR.
  • To highlight new possibilities for biomolecular characterization enabled by proton detection.
  • To showcase advancements in chemical-shift assignment, structure calculation, and dynamics assessment using protons.

Main Methods:

  • Development of techniques for enhanced proton detection in ssNMR.
  • Utilizing partial sample deuteration to reduce proton spin density.
  • Employing faster magic-angle spinning (MAS) with micro-rotor frequencies up to 130 kHz.
  • Leveraging proton chemical shifts and high gyromagnetic ratio for spatial and dynamic information.

Main Results:

  • Achieved high-resolution proton detection, overcoming previous obstacles.
  • Demonstrated facilitated chemical-shift assignment for protein backbone and side chains.
  • Enabled structure calculation and dynamics assessment in solid proteins using proton-based information.
  • Significantly reduced sample amount requirements for ssNMR analysis.
  • Expanded the scope of ssNMR to increasingly complex and higher molecular weight biomolecules.

Conclusions:

  • Proton detection in ssNMR overcomes sensitivity and resolution limitations.
  • This technique revolutionizes biomolecular characterization by providing enhanced accuracy and speed.
  • ssNMR is now capable of accessing complex cellular molecules, elucidating their functions and interactions.