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Related Concept Videos

Double Resonance Techniques: Overview01:12

Double Resonance Techniques: Overview

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...
NMR Spectrometers: Resolution and Error Correction01:14

NMR Spectrometers: Resolution and Error Correction

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...
2D NMR: Overview of Homonuclear Correlation Techniques01:16

2D NMR: Overview of Homonuclear Correlation Techniques

Homonuclear correlation spectroscopy (COSY) is a powerful technique used in Nuclear Magnetic Resonance (NMR) spectroscopy to study the correlations between nuclei of the same type within a molecule. It provides information about scalar couplings between adjacent nuclei, which helps determine connectivity and structural information. There are several COSY variants, each with its unique strengths and experimental parameters.
COSY90 is the standard two-dimensional (2D) COSY experiment that...
NMR Spectrometers: Radiofrequency Pulses and Pulse Sequences01:17

NMR Spectrometers: Radiofrequency Pulses and Pulse Sequences

A pulse is a short burst of radio waves distributed over a range of frequencies that simultaneously excites all the nuclei in the sample. Upon passing a radio frequency pulse along the x-axis, the nuclei absorb energy corresponding to their Larmor frequencies and achieve resonance. This shifts the net magnetization vector from the z-axis toward the transverse plane. This angle of rotation of the magnetization vector, or the flip angle, is proportional to the duration and intensity of the pulse.
NMR Spectrometers: Overview01:20

NMR Spectrometers: Overview

NMR spectrometers consist of a strong magnet, a radiofrequency transmitter, and a detector attached to a computer console for recording spectra of samples containing NMR-active nuclei. In first-generation NMR instruments called continuous-wave spectrometers, the resonance frequencies of the nuclei are determined by frequency-sweep or field-sweep methods. The magnetic field strength is fixed and the rf signal is swept in the former, while the radiofrequency signal is fixed and the magnetic field...
2D NMR: Overview of Heteronuclear Correlation Techniques01:18

2D NMR: Overview of Heteronuclear Correlation Techniques

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 axis.

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NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
09:25

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

An efficient (1)H/(31)P double-resonance solid-state NMR probe that utilizes a scroll coil.

Christopher V Grant1, Siu-Ling Sit, Anna A De Angelis

  • 1Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093-0307, USA.

Journal of Magnetic Resonance (San Diego, Calif. : 1997)
|August 28, 2007
PubMed
Summary

A novel scroll coil double-resonance probe enhances solid-state Nuclear Magnetic Resonance (NMR) for stationary samples. This probe offers high efficiency and minimal radiofrequency heating, proving effective for biological samples like peptides in lipid bilayers.

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15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale
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Last Updated: Jul 12, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
09:25

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale
08:09

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale

Published on: April 19, 2021

Area of Science:

  • Solid-state Nuclear Magnetic Resonance (NMR) spectroscopy
  • Biophysical chemistry
  • Materials science

Background:

  • Solid-state NMR requires specialized probes for high-frequency nuclei like proton (1H) and phosphorus-31 (31P).
  • Existing probes can face challenges with sample tuning, radiofrequency (RF) heating, and RF homogeneity, especially for complex biological samples.

Purpose of the Study:

  • To describe the construction and performance of a novel scroll coil double-resonance probe for solid-state NMR.
  • To highlight the advantages of this probe for analyzing stationary, particularly aqueous and high dielectric, biological samples.

Main Methods:

  • Construction of a scroll coil double-resonance probe designed for high resonance frequencies.
  • Incorporation of a cable tie cinch for enhanced mechanical stability of the coil.
  • Experimental validation using a Hunter Killer Peptide 1 (HKP1) interacting with phospholipid bilayers of varying lipid composition.

Main Results:

  • The scroll coil probe demonstrates high efficiency and excellent RF homogeneity.
  • It exhibits minimal perturbation of tuning across a wide range of samples.
  • Minimal RF sample heating was observed for high dielectric biopolymer samples in aqueous solution.

Conclusions:

  • The developed scroll coil probe is highly effective for solid-state NMR analysis of challenging samples, including lossy aqueous biological systems.
  • The probe's design overcomes limitations of conventional probes regarding RF heating and tuning stability.
  • This technology advances the study of biomolecular interactions, such as peptide-lipid interactions, using solid-state NMR.