NMR spectra of a microcrystalline protein at 30 kHz MAS.
Proteins are not always available in amounts desirable for solid-state magic-angle spinning (MAS) nuclear-magnetic resonance (NMR) spectroscopy. To maximize the signal-to-noise ratio achievable with small samples, the filling factor must be optimized by using small-diameter MAS rotors. These rotors have the added benefit of allowing higher radio frequency field amplitudes during polarization transfer steps and during decoupling periods as well as allowing higher spinning frequencies. We demonstrate the advantages of relatively fast MAS (30 kHz using a 2.5 mm rotor) compared to MAS at 12 kHz for the 10.4 kDa model protein Crh with 93 residues and show that the signal-to-noise ratio in two-dimensional correlation spectra can be significantly improved by taking advantage of optimized pulse sequences available with rapid MAS.
Ernst
Matthias
M
Physical Chemistry, ETH Zurich, CH-8093 Zürich, Switzerland.
Detken
Andreas
A
Böckmann
Anja
A
Meier
Beat H
BH
D001412:Bacillus subtilis; D001426:Bacterial Proteins / Q000737:chemistry*; D002247:Carbon Isotopes; D018360:Crystallography, X-Ray; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010750:Phosphoproteins / Q000737:chemistry*
D001426:Bacterial Proteins; D002247:Carbon Isotopes; C118042:Crh protein, Bacillus subtilis; D010750:Phosphoproteins