Polarization-enhanced NMR spectroscopy of biomolecules in frozen solution.
Large dynamic nuclear polarization signal enhancements (up to a factor of 100) were obtained in the solid-state magic-angle spinning nuclear magnetic resonance (NMR) spectra of arginine and the protein T4 lysozyme in frozen glycerol-water solutions with the use of dynamic nuclear polarization. Polarization was transferred from the unpaired electrons of nitroxide free radicals to nuclear spins through microwave irradiation near the electron paramagnetic resonance frequency. This approach may be a generally applicable signal enhancement scheme for the high-resolution solid-state NMR spectroscopy of biomolecules.
Hall
D A
DA
Francis Bitter Magnet Laboratory and Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Maus
D C
DC
Gerfen
G J
GJ
Inati
S J
SJ
Becerra
L R
LR
Dahlquist
F W
FW
Griffin
R G
RG
D001120:Arginine / Q000737:chemistry*; D017122:Bacteriophage T4 / Q000201:enzymology; D003497:Cyclic N-Oxides; D004583:Electrons; D005609:Free Radicals; D005615:Freezing; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008872:Microwaves; D009113:Muramidase / Q000737:chemistry*; D012996:Solutions; D013113:Spin Labels
D003497:Cyclic N-Oxides; D005609:Free Radicals; D012996:Solutions; D013113:Spin Labels; C015527:4-amino-TEMPO; D001120:Arginine; D009113:Muramidase