Accurate measurement of one-bond H-X heteronuclear dipolar couplings in MAS solid-state NMR.
J Magn Reson. 2011 Mar 21;
Authors: Schanda P, Meier BH, Ernst M
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.
PMID: 21482161 [PubMed - as supplied by publisher]
Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion.
Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion.
Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion.
Angew Chem Int Ed Engl. 2011 Sep 14;
Authors: Schanda P, Huber M, Boisbouvier J, Meier BH, Ernst M
PMID: 21915969
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Accurate Measurement of One-Bond H-X Heteronuclear Dipolar Couplings in MAS Solid-State NMR
Accurate Measurement of One-Bond H-X Heteronuclear Dipolar Couplings in MAS Solid-State NMR
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 21 March 2011</br>
Paul, Schanda , Beat H., Meier , Matthias, Ernst</br>
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...
[NMR paper] Rapid and accurate structure determination of coiled-coil domains using NMR dipolar couplings: application to cGMP-dependent protein kinase Ialpha.
Rapid and accurate structure determination of coiled-coil domains using NMR dipolar couplings: application to cGMP-dependent protein kinase Ialpha.
Related Articles Rapid and accurate structure determination of coiled-coil domains using NMR dipolar couplings: application to cGMP-dependent protein kinase Ialpha.
Protein Sci. 2005 Sep;14(9):2421-8
Authors: Schnell JR, Zhou GP, Zweckstetter M, Rigby AC, Chou JJ
Coiled-coil motifs play essential roles in protein assembly and molecular recognition, and are therefore the targets of many ongoing...
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[NMR paper] An NMR experiment for the accurate measurement of heteronuclear spin-lock relaxation
An NMR experiment for the accurate measurement of heteronuclear spin-lock relaxation rates.
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J Am Chem Soc. 2002 Sep 11;124(36):10743-53
Authors: Korzhnev DM, Skrynnikov NR, Millet O, Torchia DA, Kay LE
Rotating-frame relaxation rates, R(1)(rho), are often measured in NMR studies of protein dynamics. We show here that large systematic errors can be introduced into measured values of heteronuclear R(1)(rho) rates using schemes which are...
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11-24-2010 08:58 PM
HNCO-based measurement of one-bond amide 15N-1H couplings with optimized precision
Abstract A pair of 3D HNCO-based experiments have been developed with the aim of optimizing the precision of measurement of 1JNH couplings. Both pulse sequences record 1JNH coupling evolution during the entire constant time interval that 15N magnetization is dephasing or rephasing with respect to the directly bonded 13Cā?² nucleus, with 15N13Cā?² multiple quantum coherence maintained during the 13Cā?² evolution period. The first experiment, designed for smaller proteins, produces an apparent doubling of the 1JNH coupling without any accompanying increases in line width. The second experiment...
Accurate measurement of one-bond H-X heteronuclear dipolar couplings in MAS solid-state NMR.
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