Proton Nuclear Magnetic Resonance

Proton nuclear magnetic resonance (¹H NMR) is an analytical technique that characterizes hydrogen-containing molecules by measuring how their nuclei respond to a magnetic field and radiofrequency energy. In a strong magnetic field, hydrogen nuclei adopt quantized spin states; radiofrequency pulses perturb these states, and the resulting resonance frequencies, chemical shifts, and signal intensities reflect molecular environments and concentrations. In bioengineering, ¹H NMR supports metabolite profiling, biomolecular structure analysis, reaction monitoring, and assessment of engineered tissues or bioprocesses. Because it can analyze complex samples with limited preparation, the method links molecular composition to biological function and process performance.

Proton Nuclear Magnetic Resonance - Related Videos

Education

JoVE Science Education - Chemistry

Nuclear Magnetic Resonance (NMR) Spectroscopy

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2023

Source: Laboratory of Dr. Henrik Sundén – Chalmers University of Technology Nuclear magnetic resonance (NMR) spectroscopy is a vital analysis technique for organic chemists. With the help of NMR, the work in the organic lab has been facilitated tremendously. Not only can it provide information about the structure of a molecule but also determine the content and purity of a sample. Compared with other commonly encountered techniques for organic chemists — such as thermal analysis and mass...

Research

JoVE EoE - Spectroscopy Techniques

Nuclear Magnetic Resonance Spectroscopy to Identify Multiple Phosphorylations in Proteins

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2025

This video demonstrates the use of nuclear magnetic resonance spectroscopy (NMR) techniques to identify multiple phosphorylations in a protein. The phosphorylation of a protein at specific amino acid causes the deshielding of the neighboring amide hydrogen, which generates the spectral difference.

Nuclear Magnetic Resonance to Study Atomic Level Protein-Protein Interactions

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2025

This video describes the nuclear magnetic resonance spectroscopy technique to study protein-protein interactions between 15N-labeled wild-type and mutant envoplakin proteins and the unlabeled vimentin protein. The successful interaction between wild-type envoplakin and vimentin leads to extensive line broadening and peak disappearance in the NMR spectra, whereas the absence of an interaction between the mutated envoplakin and vimentin results in well-resolved peaks in the NMR spectra.

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

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Cited by 25 •

2016

We describe here a method to identify multiple phosphorylations of an intrinsically disordered protein by Nuclear Magnetic Resonance Spectroscopy (NMR), using Tau protein as a case study. Recombinant Tau is isotopically enriched and modified in vitro by a kinase prior to data acquisition and analysis.

Concentration of Metabolites from Low-density Planktonic Communities for Environmental Metabolomics using Nuclear Magnetic Resonance Spectroscopy

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Cited by 15 •

2012

A method for metabolite extraction from microbial planktonic communities is presented. Whole community sampling is achieved by filtration onto specially prepared filters. After lyophilization, aqueous-soluble metabolites are extracted. This approach allows for application of environmental metabolomics to trans-omics investigations of natural or experimental microbial communities.

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