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

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

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...
Double Resonance Techniques: Overview01:12

Double Resonance Techniques: Overview

Double resonance techniques in Nuclear Magnetic Resonance (NMR) spectroscopy involve the simultaneous application of two different frequencies or radiofrequency pulses to manipulate and observe two distinct nuclear spins. One important application of double resonance is spin decoupling, which selectively suppresses coupling with one type of nucleus while observing the NMR signal from another nucleus, simplifying the spectrum and enhancing resolution.
Spin decoupling is usually achieved by...
¹H NMR of Labile Protons: Temporal Resolution01:10

¹H NMR of Labile Protons: Temporal Resolution

Protons bonded to heteroatoms such as nitrogen and oxygen exhibit a range of chemical shift values. This is due to the varying degree of hydrogen bonding between the proton and the heteroatom in other molecules. The extent of hydrogen bonding affects the electron density around the proton, thereby giving different chemical shift values for the protons in the proton NMR spectrum.
The –OH proton in alcohols typically appears in the range of δ 2 to 5 ppm but can vary depending on the specific...
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...
Interpreting ¹H NMR Signal Splitting: The (n + 1) Rule01:10

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

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 others.
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...

You might also read

Related Articles

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

Sort by
Same author

The tRNA moieties of both aminoacyl-tRNA substrates of a cyclodipeptide synthase share a common binding site, as revealed by RNA microhelices mimicking tRNA acceptor arms.

Nucleic acids research·2026
Same author

Decoding mEos4b day-long maturation and engineering fast-maturing variants.

Protein science : a publication of the Protein Society·2025
Same author

Identification of uranyl-binding proteins in Arabidopsis thaliana cells exposed to uranium: Insights from a metalloproteomic analysis and characterization of Glycine-Rich RNA-binding protein 7 (GRP7).

Journal of hazardous materials·2025
Same author

Allosteric coupling between a lipid bilayer and a membrane protein.

Biophysical journal·2025
Same author

PRESERVE: adding variable flip-angle excitation to transverse relaxation-optimized NMR spectroscopy.

Magnetic resonance (Gottingen, Germany)·2025
Same author

NMR Structural Characterization of SARS-CoV-2 ORF6 Reveals an N-Terminal Membrane Anchor.

Journal of the American Chemical Society·2025

Related Experiment Video

Updated: May 26, 2026

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

Fast protein backbone NMR resonance assignment using the BATCH strategy.

Bernhard Brutscher1, Ewen Lescop

  • 1Institut de Biologie Structurale - Jean-Pierre Ebel, CNRS, CEA, UJF, UMR5075, Grenoble Cedex, France.

Methods in Molecular Biology (Clifton, N.J.)
|December 15, 2011
PubMed
Summary

We developed the BATCH strategy for rapid protein backbone resonance assignment using Nuclear Magnetic Resonance (NMR). This method significantly reduces data collection and analysis time from days to hours, enabling studies of unstable proteins.

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

Related Experiment Videos

Last Updated: May 26, 2026

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

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:

  • Structural Biology
  • Biophysical Chemistry
  • Nuclear Magnetic Resonance (NMR) Spectroscopy

Background:

  • Protein structure and dynamics are crucial for function.
  • Nuclear Magnetic Resonance (NMR) is a powerful tool for probing biomolecular details.
  • Current NMR backbone resonance assignment protocols are time-consuming, limiting applications.

Purpose of the Study:

  • To introduce and describe the BATCH strategy for accelerated protein backbone resonance assignment.
  • To demonstrate the practical implementation of BATCH for rapid NMR analysis.
  • To overcome limitations of traditional NMR assignment methods for unstable proteins and high-throughput studies.

Main Methods:

  • Utilized a combination of NMR tools: BEST/ASCOM/Targeted-Sampling/COBRA/HADAMAC.
  • Implemented time-optimized and automated data acquisition, processing, and analysis.
  • Applied the BATCH strategy to small globular proteins under favorable conditions.

Main Results:

  • Achieved backbone resonance assignment in a few hours, a significant reduction from several days.
  • Demonstrated the robustness of the BATCH strategy for NMR data analysis.
  • Enabled faster characterization of protein structure and dynamics.

Conclusions:

  • The BATCH strategy offers a substantial advancement in NMR-based protein analysis.
  • This method facilitates the study of previously challenging protein systems.
  • BATCH is poised to enhance high-throughput structural biology applications.