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

Applications Of NMR In Biology01:25

Applications Of NMR In Biology

4.2K
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.
4.2K
NMR Spectrometers: Overview01:20

NMR Spectrometers: Overview

1.7K
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...
1.7K
NMR Spectroscopy of Aromatic Compounds01:14

NMR Spectroscopy of Aromatic Compounds

5.6K
Aromatic compounds can be identified or analyzed using proton NMR and carbon‐13 NMR. Typically, aromatic hydrogens or hydrogens directly bonded to the aromatic rings are strongly deshielded by the aromatic ring current. Therefore, they absorb in the range of 6.5–8.0 ppm in proton NMR spectra. For instance, aromatic hydrogens directly bonded to the benzene ring absorb at 7.3 ppm. However, aromatic hydrogens of larger rings absorb farther upfield or downfield than the ideal range.
5.6K
Chemical Shift: Internal References and Solvent Effects01:17

Chemical Shift: Internal References and Solvent Effects

1.1K
In an NMR sample, precise measurement of the absolute absorption frequencies of nuclei is difficult. A standard internal reference compound is added, and the frequency difference between the reference signal and sample signals is measured.
The internal reference compound generally used in NMR spectroscopy is tetramethylsilane (TMS). TMS is preferred because it is chemically inert, soluble in NMR solvents, and easily removable. Also, the highly shielded methyl protons in TMS yield an intense...
1.1K

You might also read

Related Articles

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

Sort by
Same author

Probing the Conformation of BamC and BamE in Native Bacterial Membranes Using Solid-State NMR Spectroscopy.

Journal of the American Chemical Society·2026
Same author

Infiltrated penile papules as a cutaneous manifestation of disseminated BCGitis: A rare dermatologic presentation.

International journal of STD & AIDS·2025
Same author

Unlocking the Potential of Marine Sidestreams in the Blue Economy: Lessons Learned from the EcoeFISHent Project on Fish Collagen.

Marine biotechnology (New York, N.Y.)·2025
Same author

A DNP-Supported Solid-State NMR Approach to Study Nucleic Acids In Situ Reveals Berberine-Stabilized Hoogsteen Structures in Mitochondria.

Angewandte Chemie (International ed. in English)·2025
Same author

Ubiquitin's Conformational Heterogeneity as Discerned by Nuclear Magnetic Resonance Spectroscopy.

Chembiochem : a European journal of chemical biology·2024
Same author

Molecular structure and composition elucidation of an industrial humin and its fractions.

Green chemistry : an international journal and green chemistry resource : GC·2024
Same journal

Author Correction: Direct inoculation of bioreactor-controlled stirred suspension culture with cryopreserved human pluripotent stem cells.

Nature protocols·2026
Same journal

High-throughput measurements of protein domain functions using magnetic separation.

Nature protocols·2026
Same journal

Inducing physiological polarity and performing gene editing using CRISPR-Cas9 in human trophoblast organoids.

Nature protocols·2026
Same journal

Photocatalytic low-temperature defluorination of PTFE.

Nature protocols·2026
Same journal

Multimodal imaging and quantification of lanthanide chelate-labeled micro- and nanoplastics in plants.

Nature protocols·2026
Same journal

Facilitating structure-based drug discovery with an artificial intelligence-driven virtual screening platform.

Nature protocols·2026
See all related articles

Related Experiment Video

Updated: Nov 21, 2025

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

15.8K

Characterizing proteins in a native bacterial environment using solid-state NMR spectroscopy.

Siddarth Narasimhan1,2, Cecilia Pinto1,3, Alessandra Lucini Paioni1

  • 1NMR Spectroscopy, Bijvoet Center for Biomolecular Research, Utrecht University, Utrecht, the Netherlands.

Nature Protocols
|January 14, 2021
PubMed
Summary
This summary is machine-generated.

This study presents a 3-5 day protocol for preparing bacterial samples for solid-state nuclear magnetic resonance (ssNMR) studies. The method enables detailed analysis of soluble, insoluble, and membrane proteins in their native cellular environment.

More Related Videos

Author Spotlight: Unveiling the Structural and Dynamic Aspects of Glycan Molecular Recognition
07:40

Author Spotlight: Unveiling the Structural and Dynamic Aspects of Glycan Molecular Recognition

Published on: May 17, 2024

1.7K
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

12.4K

Related Experiment Videos

Last Updated: Nov 21, 2025

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

15.8K
Author Spotlight: Unveiling the Structural and Dynamic Aspects of Glycan Molecular Recognition
07:40

Author Spotlight: Unveiling the Structural and Dynamic Aspects of Glycan Molecular Recognition

Published on: May 17, 2024

1.7K
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

12.4K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Solid-state nuclear magnetic resonance (ssNMR) is a powerful technique for analyzing biomolecular structure and dynamics.
  • Studying proteins in their native cellular environment presents challenges due to their diverse solubility and localization.

Purpose of the Study:

  • To provide a detailed protocol for preparing bacterial cell samples for high-resolution and high-sensitivity ssNMR.
  • To enable the study of both soluble and insoluble/membrane-associated proteins using ssNMR.

Main Methods:

  • Utilizes Escherichia coli (DE3) strains transformed with inducible protein expression plasmids.
  • Employs minimal media (M9) growth, targeted protein labeling via rifampicin inhibition of RNA polymerase, and cell harvesting.
  • Prepares samples for conventional 13C/15N-detected ssNMR, as well as dynamic nuclear polarization (DNP) or proton (1H) detection schemes.

Main Results:

  • Successfully developed a biochemical preparation scheme for obtaining cellular samples of diverse protein types.
  • The protocol is adaptable for whole cells, cell envelopes, or isolated membrane preparations.
  • The entire preparation procedure takes an estimated 3-5 days.

Conclusions:

  • This protocol facilitates the investigation of proteins in their native settings using advanced ssNMR techniques.
  • It offers novel opportunities for studying protein structure and dynamics irrespective of molecular tumbling rates.
  • The method is suitable for a wide range of protein types and ssNMR detection schemes.