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

¹³C NMR: ¹H–¹³C Decoupling01:04

¹³C NMR: ¹H–¹³C Decoupling

1.0K
The probability of having two carbon-13 atoms next to each other is negligible because of the low natural abundance of carbon-13. Consequently, peak splitting due to carbon-carbon spin-spin coupling is not observed in spectra. However, protons up to three sigma bonds away split the carbon signal according to the n+1 rule, resulting in complicated spectra.
A broadband decoupling technique is used to simplify these complex, sometimes overlapping, signals. Broadband decoupling relies on a...
1.0K
Double Resonance Techniques: Overview01:12

Double Resonance Techniques: Overview

191
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...
191

You might also read

Related Articles

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

Sort by
Same author

A Rigid Supramolecular Solution to a Flexible Problem: A Multifunctional Calix[4]arene-Based Strategy to Prevent α‑Synuclein Toxicity.

ACS central science·2026
Same author

Molecular Interplay of Small Molecules and Calcium Ions with α-Synuclein Revealed by NMR and Molecular Dynamics Simulations.

ACS chemical neuroscience·2026
Same author

At the core of the interaction: Probing charged side chains in flexible protein regions with simultaneous nuclear magnetic resonance experiments.

Protein science : a publication of the Protein Society·2026
Same author

Toward a unified framework for determining conformational ensembles of disordered proteins.

Nature methods·2026
Same author

Human cells for human proteins: Isotope labeling in mammalian cells in suspension for functional NMR studies.

Protein science : a publication of the Protein Society·2026
Same author

Oligomerization enables the selective targeting of an intrinsically disordered region by a small molecule.

Science advances·2026

Related Experiment Video

Updated: Jun 11, 2025

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

1.2K

Disentangling the Complexity in Protein Complexes Using Complementary Isotope-Labeling and Multiple-Receiver NMR

Sonja Knödlstorfer1,2, Marco Schiavina3, Maria Anna Rodella3

  • 1Department of Structural and Computational Biology, Max Perutz Laboratories, University of Vienna, Campus Vienna Biocenter, 5, 1030 Vienna, Austria.

Journal of the American Chemical Society
|October 7, 2024
PubMed
Summary

This study introduces a novel NMR spectroscopy method using complementary isotope labeling to map protein-protein binding sites. This technique enhances the study of intrinsically disordered proteins and their interactions, like the Myc/MAX and BRCA1 complex.

More Related Videos

A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry
08:04

A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry

Published on: March 13, 2014

12.2K
Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
10:01

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

19.6K

Related Experiment Videos

Last Updated: Jun 11, 2025

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

1.2K
A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry
08:04

A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry

Published on: March 13, 2014

12.2K
Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
10:01

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

19.6K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biophysics

Background:

  • Intrinsically disordered proteins (IDPs) are crucial in eukaryotic systems but challenging pharmacological targets.
  • Nuclear Magnetic Resonance (NMR) spectroscopy offers atomistic insights into protein interactions but faces challenges like spectral overlap and sample limitations.
  • Studying IDPs and their interactions is vital for understanding cellular processes and developing new therapeutics.

Purpose of the Study:

  • To develop a novel NMR-based approach for simultaneously mapping protein-protein binding sites on interacting partners.
  • To overcome limitations of traditional NMR methods in studying complex protein interactions, particularly for IDPs.
  • To demonstrate the utility of the proposed method using a biologically significant protein complex.

Main Methods:

  • Employing a complementary isotope-labeling strategy with differential labeling of interacting partners (e.g., 15N,2H and 13C,1H).
  • Utilizing a multiple receiver NMR detection scheme for enhanced signal clarity and reduced spectral overlap.
  • Applying proton and carbon detection to obtain clean and interpretable data for binding site identification.

Main Results:

  • Successfully mapped protein-protein binding sites on two interacting partners simultaneously.
  • Obtained clean and easily readable NMR data, overcoming spectral complexity issues.
  • Demonstrated the method's effectiveness on a 50 kDa ternary complex involving Myc/MAX and BRCA1.

Conclusions:

  • The proposed NMR approach enables efficient and simultaneous mapping of protein-protein binding sites.
  • This method significantly improves the study of intrinsically disordered proteins and their interactions.
  • The technique provides a valuable tool for drug discovery targeting protein-protein interactions.