Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Two-Dimensional (2D) NMR: Overview01:12

Two-Dimensional (2D) NMR: Overview

669
The 1D NMR spectrum of large and complex molecules like natural products has complicated splitting patterns and overlapping signals, which can be easily interpreted using 2-dimensional (2D) NMR. Unlike 1D NMR, 2D NMR has two frequency axes that provide the coupling information between the nucleus A and nucleus B in a molecule. The process from which 2D spectra are obtained has four steps.
The first step is the preparation period, during which nucleus A is excited with a radiofrequency pulse....
669
NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

1.4K
The spin state of an NMR-active nucleus can have a slight effect on its immediate electronic environment. This effect propagates through the intervening bonds and affects the electronic environments of NMR-active nuclei up to three bonds away; occasionally, even farther. This phenomenon is called spin–spin coupling or J-coupling. Coupling interactions are mutual and result in small changes in the absorption frequencies of both nuclei involved. While nuclei of the same element are involved...
1.4K
¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

1.0K
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...
1.0K
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

841
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...
841
Applications Of NMR In Biology01:25

Applications Of NMR In Biology

3.7K
Nuclear magnetic resonance (NMR) spectroscopy is a very valuable analytical technique for researchers. It has been used for more than 50 years as an analytical tool. F. Bloch and E. Purcell formulated NMR in 1946 and won the 1952 Nobel Prize in Physics  for their work. Biological macromolecules such as proteins, nucleic acids, lipids, and organic molecules including pharmaceutical compounds, can be studied using this versatile tool that exploits the magnetic properties of certain nuclei.
3.7K
Interpreting ¹H NMR Signal Splitting: The (n + 1) Rule01:10

Interpreting ¹H NMR Signal Splitting: The (n + 1) Rule

1.3K
In the AX proton spin system, proton A can sense the two spin states of a coupled proton X, resulting in a doublet NMR signal with two peaks of equal (1:1) intensity. When proton A is coupled to two equivalent protons (AX2 spin system), the spin states of each X can be aligned with or against the external field, creating three possible scenarios. This results in a 1:2:1  triplet signal, where the central peak corresponds to the chemical shift of A and is twice as large or intense as the...
1.3K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Tumor-Infiltrating mregDCs Restrain Anti-Tumor Immunity in Early Relapse HCC.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2026
Same author

Two stable gut microbiome guilds predict liver tumor class and treatment responses.

iMeta·2026
Same author

TDP-DETR: Temporal dynamics perception framework for video moment retrieval and highlight detection.

Neural networks : the official journal of the International Neural Network Society·2026
Same author

<i>J</i>-Resolved Molecular Fingerprinting by Parahydrogen Hyperpolarized Low-Field NMR.

Journal of the American Chemical Society·2026
Same author

Mussel-Inspired Catechol-Functionalized Redox-Active Polypeptides for Energy Applications.

Biomacromolecules·2026
Same author

Label-Free Measurement of Ligand Interactions Using SABRE Hyperpolarization at Low Magnetic Fields.

Analytical chemistry·2026

Related Experiment Video

Updated: Jul 3, 2025

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
09:25

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

Published on: November 1, 2024

1.9K

Analysis of Large Data Sets in a Physical Chemistry Laboratory NMR Experiment Using Python.

Zefan Zhang1, Anshul Gautam1, Soon-Mi Lim1

  • 1Department of Chemistry, Texas A&M University, 3255 TAMU, College Station, Texas 77843, United States.

Journal of Chemical Education
|February 15, 2024
PubMed
Summary
This summary is machine-generated.

This study introduces a new Python-based protocol for analyzing low-field nuclear magnetic resonance (NMR) spectroscopy data in undergraduate physical chemistry labs. It equips students with essential data analysis skills for large datasets, crucial for modern science and engineering.

More Related Videos

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

12.1K
15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the &#181;s-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

5.2K

Related Experiment Videos

Last Updated: Jul 3, 2025

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
09:25

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

Published on: November 1, 2024

1.9K
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

12.1K
15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the &#181;s-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

5.2K

Area of Science:

  • Physical Chemistry Education
  • Spectroscopy Techniques
  • Computational Chemistry

Background:

  • Traditional undergraduate chemistry curricula often lack comprehensive training in large dataset analysis.
  • Nuclear Magnetic Resonance (NMR) spectroscopy is a fundamental technique in chemistry, but its application in undergraduate labs can be limited by data processing complexity.
  • There is a growing need for accessible, modern computational tools in chemistry education to prepare students for research and industry.

Purpose of the Study:

  • To present an updated experimental protocol for low-field NMR spectroscopy suitable for undergraduate physical chemistry laboratories.
  • To develop and implement a Python-based data processing and analysis workflow for this NMR experiment.
  • To introduce students to essential data analysis methodologies relevant to science and engineering through an interactive JupyterLab environment.

Main Methods:

  • Implementation of a Python-based data analysis protocol within JupyterLab interactive worksheets.
  • Utilizing low-field Nuclear Magnetic Resonance (NMR) spectroscopy for data acquisition.
  • Step-by-step interactive data handling and analysis guided by the developed protocol.

Main Results:

  • Successful integration of a Python protocol for processing and analyzing low-field NMR data.
  • Students gain hands-on experience with modern data analysis techniques using Python.
  • The protocol enhances the educational value of NMR spectroscopy experiments by incorporating computational analysis.

Conclusions:

  • The developed Python protocol effectively supports low-field NMR spectroscopy analysis in undergraduate physical chemistry labs.
  • This approach bridges the gap in data analysis training within traditional chemistry education.
  • The open-source nature of Python and JupyterLab promotes accessibility and adoption in educational settings.