1H-1H MAS correlation spectroscopy and distance measurements in a deuterated peptide.
In this Communication, we demonstrate the use of deuteration together with back substitution of exchangeable protons as a means of attenuating the strong 1H-1H couplings that broaden 1H magic angle spinning (MAS) spectra of solids. The approach facilitates 15N-1H correlation experiments as well as experiments for the measurement of 1H-1H distances. The distance measurement relies on the excellent resolution in the 1H MAS spectrum and homonuclear double quantum recoupling techniques. The 1H-1H dipolar recoupling can be analyzed in an analytical fashion by fitting the data to a 2- or 3-spin system. The experiments are performed on a sample of the dipeptide N-Ac-Val-Leu-OH, which was synthesized from uniformly [2H, 15N] labeled materials and back-exchanged in H2O.
Reif
B
B
Department of Chemistry and MIT/Harvard Center for Magnetic Resonance, Francis Bitter Magnet Laboratory, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
Jaroniec
C P
CP
Rienstra
C M
CM
Hohwy
M
M
Griffin
R G
RG
D003903:Deuterium; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008433:Mathematics; D008968:Molecular Conformation; D010455:Peptides / Q000737:chemistry*; D012815:Signal Processing, Computer-Assisted
D010455:Peptides; D003903:Deuterium