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

Double Resonance Techniques: Overview01:12

Double Resonance Techniques: Overview

293
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...
293
Insensitive Nuclei Enhanced by Polarization Transfer (INEPT)01:15

Insensitive Nuclei Enhanced by Polarization Transfer (INEPT)

506
Insensitive Nuclei Enhanced by Polarization Transfer (INEPT) is an advanced Nuclear Magnetic Resonance (NMR) technique specifically designed to detect and enhance the signals of low-abundance nuclei, such as carbon-13 and nitrogen-15, in small molecules. The fundamental principle behind INEPT is the transfer of polarization from a more abundant and highly polarizable nucleus, typically hydrogen-1, to the low-abundance nucleus of interest. This process effectively boosts the NMR signal of the...
506
Other Nuclides: 31P, 19F, 15N NMR01:16

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

465
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...
465
Atomic Nuclei: Magnetic Resonance01:05

Atomic Nuclei: Magnetic Resonance

753
The number of nuclear spins aligned in the lower energy state is slightly greater than those in the higher energy state. In the presence of an external magnetic field, as the spins precess at the Larmor frequency, the excess population results in a net magnetization oriented along the z axis. When a pulse or a short burst of radio waves at the Larmor frequency is applied along the x axis, the coupling of frequencies causes resonance and flips the nuclear spins of the excess population from the...
753
Two-Dimensional (2D) NMR: Overview01:12

Two-Dimensional (2D) NMR: Overview

873
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....
873
Atomic Nuclei: Nuclear Relaxation Processes01:23

Atomic Nuclei: Nuclear Relaxation Processes

723
In the absence of an external magnetic field, nuclear spin states are degenerate and randomly oriented. When a magnetic field is applied, the spins begin to precess and orient themselves along (lower energy) or against (higher energy) the direction of the field. At equilibrium, a slight excess population of spins exists in the lower energy state. Because the direction of the magnetic field is fixed as the z-axis,  the precessing magnetic moments are randomly oriented around the z-axis.
723

You might also read

Related Articles

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

Sort by
Same author

Unlocking Gd(III) Anisotropy: Determining the Zero-Field Splitting Axes to Enhance Spin-Label Structural Analysis.

Journal of the American Chemical Society·2026
Same author

The prospective Austrian hypertrophic cardiomyopathy registry - design, methods and results of the run-in period.

Heart failure reviews·2026
Same author

Rapidly evolving aphid gall effector proteins exhibit saposin-like folds.

bioRxiv : the preprint server for biology·2026
Same author

The R203W substitution drives PACS-1 syndrome by disrupting intramolecular regulation.

The FEBS journal·2026
Same author

Sex-specific short- and long-term outcomes in patients with leadless cardiac pacemakers.

Clinical research in cardiology : official journal of the German Cardiac Society·2026
Same author

Hereditary Transthyretin Amyloidosis in Austria: Clinical, Genetic, and Demographic Insights from a Nationwide Cohort.

Journal of clinical medicine·2026

Related Experiment Video

Updated: Sep 11, 2025

Preparation of Fungal and Plant Materials for Structural Elucidation Using Dynamic Nuclear Polarization Solid-State NMR
09:37

Preparation of Fungal and Plant Materials for Structural Elucidation Using Dynamic Nuclear Polarization Solid-State NMR

Published on: February 12, 2019

7.6K

Pushing Sensitivity and Specificity Limits in Native Structural Biology: 19 F Multinuclear Dynamic Nuclear

Kumar Tekwani Movellan, Daniel Banks, Christian Reiter

    Biorxiv : the Preprint Server for Biology
    |August 12, 2025
    PubMed
    Summary

    This study introduces a highly sensitive fluorine-19 (19F) NMR method using dynamic nuclear polarization (DNP) to analyze protein structures in mammalian cells. This breakthrough enables background-free, atomic-level structural insights into proteins like Cyclophilin A within their cellular environment.

    More Related Videos

    Cryogenic Sample Loading into a Magic Angle Spinning Nuclear Magnetic Resonance Spectrometer that Preserves Cellular Viability
    06:42

    Cryogenic Sample Loading into a Magic Angle Spinning Nuclear Magnetic Resonance Spectrometer that Preserves Cellular Viability

    Published on: September 1, 2020

    3.6K
    High-Temperature and High-Pressure In situ Magic Angle Spinning Nuclear Magnetic Resonance Spectroscopy
    08:55

    High-Temperature and High-Pressure In situ Magic Angle Spinning Nuclear Magnetic Resonance Spectroscopy

    Published on: October 9, 2020

    5.7K

    Related Experiment Videos

    Last Updated: Sep 11, 2025

    Preparation of Fungal and Plant Materials for Structural Elucidation Using Dynamic Nuclear Polarization Solid-State NMR
    09:37

    Preparation of Fungal and Plant Materials for Structural Elucidation Using Dynamic Nuclear Polarization Solid-State NMR

    Published on: February 12, 2019

    7.6K
    Cryogenic Sample Loading into a Magic Angle Spinning Nuclear Magnetic Resonance Spectrometer that Preserves Cellular Viability
    06:42

    Cryogenic Sample Loading into a Magic Angle Spinning Nuclear Magnetic Resonance Spectrometer that Preserves Cellular Viability

    Published on: September 1, 2020

    3.6K
    High-Temperature and High-Pressure In situ Magic Angle Spinning Nuclear Magnetic Resonance Spectroscopy
    08:55

    High-Temperature and High-Pressure In situ Magic Angle Spinning Nuclear Magnetic Resonance Spectroscopy

    Published on: October 9, 2020

    5.7K

    Area of Science:

    • Biophysics
    • Structural Biology
    • Nuclear Magnetic Resonance Spectroscopy

    Background:

    • Understanding protein structure and interactions in cells is crucial for biology and medicine.
    • Current methods face challenges in obtaining atomic-level protein structural data within cellular contexts.

    Purpose of the Study:

    • To develop a highly sensitive and specific NMR technique for atomic-level protein structural analysis in mammalian cells.
    • To enable background-free detection and structural elucidation of target proteins in vivo.

    Main Methods:

    • A fluorine-19 (19F)-based, proton (1H)-assisted dynamic nuclear polarization (DNP) magic angle spinning (MAS) NMR approach.
    • Incorporation of a single fluorine atom into the tryptophan residue of human Cyclophilin A (CypA).
    • Utilized 1H-19F cross-polarization (CP) and 19F-13C double CP for enhanced sensitivity and structural information.

    Main Results:

    • Achieved significant sensitivity gains using 1H-19F CP-MAS NMR.
    • Obtained unique structural insights via 19F-13C double CP.
    • Demonstrated selective detection of 13C signals up to 6 Å from the fluorine label using 1H-19F-13C magnetization transfer.

    Conclusions:

    • Established a novel framework for DNP MAS NMR to investigate protein structure, dynamics, and interactions in mammalian cells.
    • The method allows for background-free, atomic-level structural analysis of proteins in their native cellular environment.
    • This technique advances the study of cellular processes and therapeutic development.