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Journal Article

Efficient CO-CA transfer in highly deuterated proteins by band-selective homonuclear cross-polarization.

MPS-Authors
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Chevelkov,  V.
Research Group of Solid-State NMR, MPI for Biophysical Chemistry, Max Planck Society;

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Giller,  K.
Department of NMR-Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Becker,  S.
Department of NMR-Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Lange,  A.
Research Group of Solid-State NMR, MPI for Biophysical Chemistry, Max Planck Society;

Fulltext (public)

1752698.pdf
(Publisher version), 929KB

Supplementary Material (public)

1752698_Supplement_1.doc
(Supplementary material), 2MB

Citation

Chevelkov, V., Giller, K., Becker, S., & Lange, A. (2013). Efficient CO-CA transfer in highly deuterated proteins by band-selective homonuclear cross-polarization. Journal of Magnetic Resonance, 230, 205-211. doi:10.1016/j.jmr.2013.02.021.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0013-78D0-7
Abstract
Robust and efficient band-selective magnetization transfer between CO and CA spins can be achieved in highly deuterated solid proteins by dipolar-based homonuclear cross polarization. The approach is designed for moderate magic-angle spinning rates and high external magnetic fields where the isotropic chemical shift difference of CO and CA considerably exceeds the spinning rate. The most efficient recoupling is achieved when the sum of effective radio-frequency fields on CO and CA resonances equals two times the spinning rate. This method can be directly implemented in proton-detected versions of inter-residual correlation experiments as needed for resonance assignment in protein solid-state NMR spectroscopy.