Coupling amplification in 2D MAS NMR and its application to torsion angle determination in peptides.
A technique for amplifying the apparent magnitudes of 13C-1H and 15N-1H dipolar interactions in magic-angle spinning experiments is described. By inserting rotor-synchronized 180 degrees pulses in the evolution period of a 2D dipolar-chemical shift experiment, heteronuclear dipolar couplings are doubled or quadrupled relative to the spinning speed. The increased number of dipolar sidebands is desirable for retaining structural information in the indirectly detected dipolar dimension while resolving inequivalent sites in the isotropic chemical shift dimension at relatively high spinning speeds. This coupling amplification method is incorporated into an experiment that determines the peptide torsion angle phi through the relative orientation of the Calpha-Halpha and N-HN bonds. It is shown both experimentally and theoretically that the angular resolution of the measurement is enhanced significantly by the selective doubling of the N-HN coupling.
Hong
M
M
Francis Bitter Magnet Laboratory and Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts, 02139, USA.
Gross
J D
JD
Rienstra
C M
CM
Griffin
R G
RG
Kumashiro
K K
KK
Schmidt-Rohr
K
K
D055598:Chemical Phenomena; D002627:Chemistry, Physical; D009682:Magnetic Resonance Spectroscopy; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation
D010455:Peptides