title: 1H-1H MAS correlation spectroscopy and distance measurements in a deuterated peptide.
abstract: 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.
authors.affiliation: Department of Chemistry and MIT/Harvard Center for Magnetic Resonance, Francis Bitter Magnet Laboratory, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
authors.forename: B
authors.initials: B
authors.lastname: Reif
authors.forename: C P
authors.initials: CP
authors.lastname: Jaroniec
authors.forename: C M
authors.initials: CM
authors.lastname: Rienstra
authors.forename: M
authors.initials: M
authors.lastname: Hohwy
authors.forename: R G
authors.initials: RG
authors.lastname: Griffin
mesh_terms: D003903:Deuterium; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008433:Mathematics; D008968:Molecular Conformation; D010455:Peptides / Q000737:chemistry*; D012815:Signal Processing, Computer-Assisted
chemical_list: D010455:Peptides; D003903:Deuterium