Efficient band-selective homonuclear CO-CA cross-polarization in protonated proteins.
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.
Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Veniamin
V
Chevelkov
Chaowei
C
Shi
Hannes Klaus
HK
Fasshuber
Stefan
S
Becker
Adam
A
Lange
D019906:Nuclear Magnetic Resonance, Biomolecular; D011506:Proteins / Q000737:chemistry*; D011522:Protons; D011846:Radio Waves; D012815:Signal Processing, Computer-Assisted; D025801:Ubiquitin / Q000737:chemistry
D011506:Proteins; D011522:Protons; D025801:Ubiquitin