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Related Concept Videos

Other Nuclides: 31P, 19F, 15N NMR01:16

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

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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...
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Double Resonance Techniques: Overview01:12

Double Resonance Techniques: Overview

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

Insensitive Nuclei Enhanced by Polarization Transfer (INEPT)

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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...
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Nuclear Overhauser Enhancement (NOE)01:07

Nuclear Overhauser Enhancement (NOE)

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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...
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¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

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Spin systems where the difference in chemical shifts of the coupled nuclei is greater than ten times J are called first-order spin systems. These nuclei are weakly coupled, and their chemical shifts and coupling constant can generally be estimated from the well-separated signals in the spectrum.
As Δν decreases and the signals move closer, the doublets appear increasingly distorted. The intensities of the inner lines increase at the cost of those of the outer lines as the signals are...
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NMR Spectrometers: Resolution and Error Correction01:14

NMR Spectrometers: Resolution and Error Correction

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When magnetic nuclei in a sample achieve resonance and undergo relaxation, the signal detected in NMR is an approximately exponential free induction decay. Fourier transform of an exponential decay yields a Lorentzian peak in the frequency domain. Lorentzian peaks in an NMR spectrum are defined by their amplitude, full width at half maximum, and position, where the peak width is governed by the spin-spin relaxation time alone. In real experiments, however, the applied magnetic field is rendered...
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Related Experiment Video

Updated: Sep 13, 2025

Preparation of Fungal and Plant Materials for Structural Elucidation Using Dynamic Nuclear Polarization Solid-State NMR
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Pushing Sensitivity and Specificity Limits in Native Structural Biology: 19F Multinuclear Dynamic Nuclear

Kumar Tekwani Movellan1,2, Daniel Banks3, Christian Reiter4

  • 1Department of Chemistry and Biochemistry, University of Delaware, Newark, Delaware 19716, United States.

Journal of the American Chemical Society
|August 4, 2025
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Summary

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

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Area of Science:

  • Biochemistry
  • Biophysics
  • Structural Biology

Background:

  • Understanding protein structure and interactions is crucial for cellular processes and drug development.
  • Determining atomic-level protein structural changes in cellular environments remains a significant challenge.
  • Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful tool for molecular structure determination.

Purpose of the Study:

  • To develop a highly sensitive and specific NMR method for atomic-level protein structural analysis in mammalian cells.
  • To overcome the limitations of traditional NMR in detecting proteins within complex cellular matrices.
  • To establish a framework for investigating protein structure, dynamics, and interactions in vivo.

Main Methods:

  • Development of a fluorine-19 (19F)-based, proton (1H)-assisted dynamic nuclear polarization (DNP) magic angle spinning (MAS) NMR technique.
  • Application of 1H-19F cross-polarization (CP) for enhanced sensitivity and 19F-13C double CP for structural information.
  • Utilizing 1H-19F-13C magnetization transfer for selective detection of protein residues near a fluorine label.

Main Results:

  • Achieved background-free detection of target proteins in mammalian cells with exceptional sensitivity and specificity.
  • Demonstrated the methodology using human Cyclophilin A (CypA) in A2780 cells, incorporating a single fluorine atom.
  • Successfully detected 13C signals from CypA residues up to 6 Å away from the fluorine label via magnetization transfer.

Conclusions:

  • The developed 19F DNP MAS NMR approach provides a sensitive and specific tool for atomic-level protein structural analysis in mammalian cells.
  • This methodology enables the investigation of protein structure, dynamics, and interactions within their native cellular context.
  • The study establishes a robust framework for advancing in vivo protein studies using NMR spectroscopy.