title: Accurate measurement of one-bond H-X heteronuclear dipolar couplings in MAS solid-state NMR.
abstract: The accurate experimental determination of dipolar-coupling constants for one-bond heteronuclear dipolar couplings in solids is a key for the quantification of the amplitudes of motional processes. Averaging of the dipolar coupling reports on motions on time scales up to the inverse of the coupling constant, in our case tens of microseconds. Combining dipolar-coupling derived order parameters that characterize the amplitudes of the motion with relaxation data leads to a more precise characterization of the dynamical parameters and helps to disentangle the amplitudes and the time scales of the motional processes, which impact relaxation rates in a highly correlated way. Here. we describe and characterize an improved experimental protocol--based on REDOR--to measure these couplings in perdeuterated proteins with a reduced sensitivity to experimental missettings. Because such effects are presently the dominant source of systematic errors in experimental dipolar-coupling measurements, these compensated experiments should help to significantly improve the precision of such data. A detailed comparison with other commonly used pulse sequences (T-MREV, phase-inverted CP, R18(2)(5), and R18(1)(7)) is provided.
authors.affiliation: Physical Chemistry, ETH Zürich, Wolfgang-Pauli-Strasse 10, 8093 Zürich, Switzerland.
authors.forename: Paul
authors.initials: P
authors.lastname: Schanda
authors.forename: Beat H
authors.initials: BH
authors.lastname: Meier
authors.forename: Matthias
authors.initials: M
authors.lastname: Ernst
mesh_terms: D016880:Anisotropy; D005583:Fourier Analysis; D006860:Hydrogen Bonding; D008962:Models, Theoretical; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D009716:Numerical Analysis, Computer-Assisted; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins