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Related Concept Videos

¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR01:15

¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR

The axial and equatorial protons in cyclohexane can be distinguished by performing a variable-temperature NMR experiment. In this process, except for one proton, the remaining eleven protons are replaced by deuterium. The deuterium substitution avoids the possible peak splitting caused by the spin-spin coupling between the adjacent protons. The remaining proton flips between the axial and equatorial positions.
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...
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...
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 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.
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...

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Related Experiment Video

Updated: Jun 12, 2026

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)
10:28

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)

Published on: November 2, 2018

Field-cycling NMR relaxometry with spatial selection.

Kerrin J Pine1, Gareth R Davies, David J Lurie

  • 1Aberdeen Biomedical Imaging Centre, University of Aberdeen, Aberdeen, Scotland, UK. k.pine@abdn.ac.uk

Magnetic Resonance in Medicine
|June 1, 2010
PubMed
Summary
This summary is machine-generated.

Fast field-cycling MRI measures T(1) dispersion curves, revealing unique tissue properties. This technique accurately maps these curves in specific volumes of protein-rich human tissue in vivo.

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

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Area of Science:

  • Magnetic Resonance Imaging (MRI)
  • Biophysics

Background:

  • Conventional MRI operates at fixed magnetic fields, limiting endogenous information acquisition.
  • T(1) dispersion curves, plotting relaxation time (T(1)) against field strength, offer unique biophysical insights.
  • Fast field-cycling MRI (FFC-MRI) enables measurements across a wide range of magnetic fields.

Purpose of the Study:

  • To develop and validate a novel pulse sequence for measuring T(1) dispersion curves in selected volumes using FFC-MRI.
  • To assess the accuracy and reliability of volume selection in T(1) dispersion measurements.

Main Methods:

  • A pulse sequence combining saturation-recovery/inversion-recovery T(1) measurements with field cycling and point-resolved spectroscopy localization was developed.
  • Volume selection was performed based on a pilot image.
  • Measurements were conducted on a whole-body FFC scanner with 59-mT detection.

Main Results:

  • The developed method accurately measures T(1) dispersion curves from selected volumes without significant loss of accuracy, even with long echo times and RF field inhomogeneity.
  • The voxel profile was consistent with the expected image slice profile.
  • Distinctive "quadrupole dips" were observed in the T(1) dispersion curves of protein-rich human tissues in vivo, indicating sensitivity to tissue composition.

Conclusions:

  • FFC-MRI with volume selection provides accurate T(1) dispersion curves.
  • This technique reveals unique "quadrupole dips" in vivo, offering new insights into the biophysical properties of protein-rich tissues.