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Journal Article

Efficient band-selective homonuclear CO-CA cross-polarization in protonated proteins.

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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Fasshuber,  H. K.
Research Group of Solid-State NMR, 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)

1836824.pdf
(Publisher version), 584KB

Supplementary Material (public)

1836824_Supplement_1.docx
(Supplementary material), 418KB

Citation

Chevelkov, V., Shi, C., Fasshuber, H. K., Becker, S., & Lange, A. (2013). Efficient band-selective homonuclear CO-CA cross-polarization in protonated proteins. Journal of Biomolecular NMR, 56(4), 303-311. doi:10.1007/s10858-013-9767-1.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0014-55AB-4
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 N(i)CO(i-1)CA(i-1) and CA(i)(N-i)CO(i-1)CA(i-1) two-dimensional interresidual correlation experiments for fast and efficient resonance assignment of ubiquitin by solid-state NMR spectroscopy.