1H-detected 1H-1H correlation spectroscopy of a stereo-array isotope labeled amino acid under fast magic-angle spinning.
The combined use of selective deuteration, stereo-array isotope labeling (SAIL), and fast magic-angle spinning effectively suppresses the 1H-1H dipolar couplings in organic solids. This method provided the high-field 1H NMR linewidths comparable to those achieved by combined rotation and multiple-pulse spectroscopy. This technique was applied to two-dimensional 1H-detected 1H-1H polarization transfer CHH experiments of valine. The signal sensitivity for the 1H-detected CHH experiments was greater than that for the 13C-detected 1H-1H polarization transfer experiments by a factor of 2-4. We obtained the 1H-1H distances in SAIL valine by CHH experiments with an accuracy of about 0.2A by using a theory developed for 1H-1H polarization transfer in 13C-labeled organic compounds.
Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
Hiroki
H
Takahashi
Masatsune
M
Kainosho
Hideo
H
Akutsu
Toshimichi
T
Fujiwara
D000465:Algorithms; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D011522:Protons; D013113:Spin Labels; D013194:Staining and Labeling; D013237:Stereoisomerism; D014633:Valine / Q000737:chemistry*
D011522:Protons; D013113:Spin Labels; D014633:Valine