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 Experiment Videos

A selective experiment for the sequential protein backbone assignment from 3D heteronuclear spectra.

Wolfgang Bermel1, Ivano Bertini, Isabella C Felli

  • 1Bruker BioSpin GmbH, Rheinstetten, Germany.

Journal of Magnetic Resonance (San Diego, Calif. : 1997)
|January 15, 2005
PubMed
Summary

Two new protonless Nuclear Magnetic Resonance (NMR) sequences enhance protein backbone assignment. These modified CANCO sequences selectively show intra-residue correlations, with one variant offering improved sensitivity for easier protein analysis.

Related Concept Videos

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

Long-lived coherences for the observation of oxidation kinetics on different timescales by NMR.

Communications chemistry·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

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

Science advances·2026
Same author

<sup>15</sup>N optimal control pulses: an efficient approach to enhance heteronuclear-detected NMR experiments at high magnetic fields.

Journal of magnetic resonance (San Diego, Calif. : 1997)·2025

Area of Science:

  • Biochemistry
  • Spectroscopy
  • Structural Biology

Background:

  • Nuclear Magnetic Resonance (NMR) spectroscopy is crucial for determining protein structure.
  • Protonless NMR techniques offer advantages for certain protein analyses.
  • The original CANCO sequence aids in protein backbone assignment but includes both inter- and intra-residue correlations.

Purpose of the Study:

  • To present two modified triple-resonance CANCO sequences.
  • To achieve selective intra-residue correlation detection.
  • To improve sensitivity for enhanced protein backbone assignment.

Main Methods:

  • Modification of the triple-resonance CANCO NMR sequence.
  • Development of two new sequence variants.
  • Utilizing protonless NMR for protein analysis.

Related Experiment Videos

Main Results:

  • The new sequences selectively display intra-residue Ca-CO correlations.
  • The original CANCO sequence showed both inter- and intra-residue correlations.
  • One modified sequence demonstrated improved sensitivity.

Conclusions:

  • The modified CANCO sequences are valuable tools for protein backbone assignment.
  • These sequences facilitate facile sequence-specific assignment using protonless NMR.
  • The selective correlation detection aids in simplifying spectral interpretation.