Related Experiment Video
Updated: May 9, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Efficient band-selective homonuclear CO-CA cross-polarization in protonated proteins
Veniamin Chevelkov1, Chaowei Shi, Hannes Klaus Fasshuber
1Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Abstract:
Previously introduced for highly deuterated proteins, band-selective magnetization transfer between CO and CA spins by dipolar-based homonuclear cross polarization is applied here to a protonated protein. Robust and efficient recoupling is achieved when the sum of effective radio-frequency fields on CO and CA resonances equals two times the spinning rate, yielding up to 33% of magnetization transfer efficiency in protonated ubiquitin. The approach is designed for moderate magic-angle spinning rates and high external magnetic fields when the isotropic chemical shift difference of CO and CA considerably exceeds the spinning rate. This method has been implemented in NiCOi-1CAi-1 and CAi(Ni)COi-1CAi-1 two-dimensional interresidual correlation experiments for fast and efficient resonance assignment of ubiquitin by solid-state NMR spectroscopy.
Related Concept Videos
2D NMR: Overview of Homonuclear Correlation Techniques
COSY90 is the standard two-dimensional (2D) COSY experiment that...
2D NMR: Overview of Heteronuclear Correlation Techniques
¹H NMR Chemical Shift Equivalence: Homotopic and Heterotopic Protons
2D NMR: Homonuclear Correlation Spectroscopy (COSY)
Proton (¹H) NMR: Chemical Shift
Absorption signals of all the protium nuclei in a...
¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)
