title: High-resolution heteronuclear correlation spectroscopy in solid state NMR of aligned samples.
abstract: A new two-dimensional scheme is proposed for accurate measurements of high-resolution chemical shifts and heteronuclear dipolar couplings in NMR of aligned samples. Both the (1)H chemical shifts and the (1)H-(15)N dipolar couplings are evolved in the indirect dimension while the (15)N chemical shifts are detected. This heteronuclear correlation (HETCOR) spectroscopy yields high-resolution (1)H chemical shifts split by the (1)H-(15)N dipolar couplings in the indirect dimension and the (15)N chemical shifts in the observed dimension. The advantages of the HETCOR technique are illustrated for a static (15)N-acetyl-valine crystal sample and a (15)N-labeled helical peptide sample aligned in hydrated lipid bilayers.
authors.affiliation: Center for Interdisciplinary Magnetic Resonance, National High Magnetic Field Laboratory, 1800 E. Paul Dirac Drive, Tallahassee, FL 32310, USA. rfu@magnet.fsu.edu
authors.forename: Riqiang
authors.initials: R
authors.lastname: Fu
authors.forename: Milton
authors.initials: M
authors.lastname: Truong
authors.forename: Randy J
authors.initials: RJ
authors.lastname: Saager
authors.forename: Myriam
authors.initials: M
authors.lastname: Cotten
authors.forename: Timothy A
authors.initials: TA
authors.lastname: Cross
mesh_terms: D000595:Amino Acid Sequence; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes; D010455:Peptides / Q000737:chemistry*; D014633:Valine / Q000031:analogs & derivatives* / Q000737:chemistry
chemical_list: D009587:Nitrogen Isotopes; D010455:Peptides; D014633:Valine; C055589:N-acetylvaline