Low-power high-resolution solid-state NMR of peptides and proteins.
We demonstrate that two-dimensional solid-state NMR chemical-shift correlation spectra can be recorded under low-power conditions. Except for the cross-polarization period, no rf-field amplitudes above 40 kHz are used. Such experiments require the use of fast (>50 kHz) magic-angle spinning (MAS). A comparison with the high-power version of the experiment shows no general line broadening but some changes in the polarization-transfer dynamics.
Ernst
Matthias
M
Physical Chemistry, ETH-Zürich, CH-8093 Zürich, Switzerland.
Meier
Marcel A
MA
Tuherm
Tiit
T
Samoson
Ago
A
Meier
Beat H
BH
D019906:Nuclear Magnetic Resonance, Biomolecular / Q000295:instrumentation / Q000379:methods*; D010456:Peptides, Cyclic / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry*
D010456:Peptides, Cyclic; D011506:Proteins; C100265:antamanide