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Related Concept Videos

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

1.0K
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...
1.0K
¹H NMR: Complex Splitting01:13

¹H NMR: Complex Splitting

1.8K
A proton M that is coupled to a proton X results in doublet signals for M. However, NMR-active nuclei can be simultaneously coupled to more than one nonequivalent nucleus. When M is coupled to a second proton A, such as in styrene oxide, each peak in the doublet is split into another doublet.
Splitting diagrams or splitting tree diagrams are routinely used to depict such complex couplings. While drawing splitting diagrams, the splitting with the larger coupling constant is usually applied...
1.8K
¹H NMR Signal Integration: Overview00:58

¹H NMR Signal Integration: Overview

3.3K
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...
3.3K
¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR01:15

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

1.7K
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.
1.7K
NMR Spectroscopy: Chemical Shift Overview01:15

NMR Spectroscopy: Chemical Shift Overview

3.1K
The position of the absorption signal of a sample is reported relative to the position of the signal of tetramethylsilane (TMS), which is added as an internal reference while recording spectra. The difference between the absorption frequencies of the sample and TMS (in Hz) is divided by the spectrometer operating frequency (in MHz) to obtain a dimensionless quantity called the chemical shift. It is reported on the δ (delta) scale and expressed in parts per million.
For instance, the proton...
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Related Experiment Video

Updated: Jan 18, 2026

Line Shape Analysis of Dynamic NMR Spectra for Characterizing Coordination Sphere Rearrangements at a Chiral Rhenium Polyhydride Complex
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Comprehensive analysis of NMR data using advanced line shape fitting.

Markus Niklasson1, Renee Otten2, Alexandra Ahlner3

  • 1Division of Chemistry, Department of Physics, Chemistry and Biology, Linköping University, 58183, Linköping, Sweden. marni@ifm.liu.se.

Journal of Biomolecular NMR
|October 19, 2017
PubMed
Summary
This summary is machine-generated.

A new version of PINT software streamlines Nuclear Magnetic Resonance (NMR) data analysis for biomolecules. This open-source tool simplifies peak picking, line shape fitting, and data extraction, enhancing productivity for researchers studying protein structure and dynamics.

Keywords:
DynamicsLine shape fittingPeak integrationRelaxationSpectral analysis

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Area of Science:

  • Biochemistry and Structural Biology
  • Computational Chemistry
  • Biophysics

Background:

  • Nuclear Magnetic Resonance (NMR) spectroscopy provides atomic-level insights into biomolecular structure and dynamics.
  • Current NMR data analysis is often fragmented and time-consuming, requiring multiple software tools.
  • Challenges exist in accurately determining spectral parameters and validating results.

Purpose of the Study:

  • To introduce an integrated, cross-platform, open-source software, PINT, for comprehensive NMR data analysis.
  • To enhance the efficiency and versatility of analyzing NMR spectra of biomolecules.
  • To provide researchers with a streamlined workflow from spectral visualization to publication-ready figures.

Main Methods:

  • Development of a redesigned PINT software with a graphical user interface.
  • Implementation of functionalities for peak picking, peak list editing, and line shape fitting.
  • Integration of tools for extracting relaxation rates, heteronuclear NOE values, and exchange parameters.

Main Results:

  • The new PINT software offers a unified platform for NMR spectral analysis, reducing reliance on multiple applications.
  • It significantly increases user productivity by automating and simplifying complex analysis steps.
  • Unique features include advanced tools for evaluating fitting quality and customizable output options.

Conclusions:

  • The redesigned PINT software provides a versatile and user-friendly solution for NMR data analysis.
  • It empowers researchers of all experience levels to efficiently obtain high-quality structural and dynamic information from biomolecular NMR spectra.
  • PINT facilitates faster preparation of publication-ready figures, accelerating scientific dissemination.