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Related Concept Videos

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.
¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)01:20

¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)

When proton-coupled carbon-13 spectra are simplified by a broadband proton decoupling technique, structural information about the coupled protons is lost. Distortionless enhancement by polarization transfer (DEPT) is a technique that provides information on the number of hydrogens attached to each carbon in a molecule. While the DEPT experiment utilizes complex pulse sequences, the pulse delay and flip angle are specifically manipulated. The resulting signals have different phases depending on...
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...
¹H NMR Signal Integration: Overview00:58

¹H NMR Signal Integration: Overview

The intensity of a signal, which can be represented by the area under the peak, depends on the number of protons contributing to that signal. The area under each peak is shown as a vertical line called an integral, with the integral value listed under it, as seen in the proton NMR spectrum of benzyl acetate. Each integral value is divided by the smallest integral value to obtain the ratio of the number of protons producing each signal. The ratio reveals the relative number of protons and not...
¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

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 slanted or...
¹³C NMR: ¹H–¹³C Decoupling01:04

¹³C NMR: ¹H–¹³C Decoupling

The probability of having two carbon-13 atoms next to each other is negligible because of the low natural abundance of carbon-13. Consequently, peak splitting due to carbon-carbon spin-spin coupling is not observed in spectra. However, protons up to three sigma bonds away split the carbon signal according to the n+1 rule, resulting in complicated spectra.
A broadband decoupling technique is used to simplify these complex, sometimes overlapping, signals. Broadband decoupling relies on a...

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Related Experiment Video

Updated: Jun 22, 2026

NMR Spectroscopy as a Robust Tool for the Rapid Evaluation of the Lipid Profile of Fish Oil Supplements
08:54

NMR Spectroscopy as a Robust Tool for the Rapid Evaluation of the Lipid Profile of Fish Oil Supplements

Published on: May 1, 2017

Clean absorption mode NMR data acquisition based on time-proportional phase incrementation.

Yibing Wu1, Arindam Ghosh, Thomas Szyperski

  • 1Department of Chemistry, The State University of New York at Buffalo, Buffalo, NY 14260, USA.

Journal of Structural and Functional Genomics
|June 6, 2009
PubMed
Summary
This summary is machine-generated.

This study introduces a new method for Nuclear Magnetic Resonance (NMR) data acquisition, yielding cleaner spectra without dispersive components. This enhances automated spectral analysis and aids in rapid structure determination.

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

Published on: November 2, 2018

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Last Updated: Jun 22, 2026

NMR Spectroscopy as a Robust Tool for the Rapid Evaluation of the Lipid Profile of Fish Oil Supplements
08:54

NMR Spectroscopy as a Robust Tool for the Rapid Evaluation of the Lipid Profile of Fish Oil Supplements

Published on: May 1, 2017

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

Area of Science:

  • Chemistry
  • Spectroscopy
  • Biophysics

Background:

  • Nuclear Magnetic Resonance (NMR) spectroscopy is crucial for molecular structure determination.
  • Existing NMR data acquisition methods can produce dispersive peaks, complicating spectral analysis.
  • Automated spectral analysis and high-throughput structure determination require cleaner NMR spectra.

Purpose of the Study:

  • To present a novel NMR data acquisition method for clean absorption mode spectra.
  • To eliminate dispersive frequency domain peak components in NMR spectra.
  • To facilitate automated spectral analysis and high-throughput NMR structure determination.

Main Methods:

  • Utilized mirrored time domain sampling.
  • Employed time-proportional phase incrementation (TPPI) for quadrature detection.
  • Developed a technique for clean absorption mode reduced-dimensionality projection NMR spectra.

Main Results:

  • Achieved NMR spectra completely devoid of dispersive frequency domain peak components.
  • Demonstrated the method's effectiveness in simplifying peak identification and maxima localization.
  • Showcased the unique value for generating clean absorption mode projection spectra.

Conclusions:

  • The presented NMR data acquisition method significantly improves spectral quality.
  • This approach overcomes limitations of current methods, enabling more reliable automated spectral analysis.
  • The technique is valuable for accelerating high-throughput NMR-based structure determination.