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.
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...
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04-13-2011 11:57 PM
[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.
Related Articles An NMR experiment for the accurate measurement of heteronuclear spin-lock relaxation rates.
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
Conformational dependence of 13C shielding and coupling constants for methionine
Abstract Methionine residues fulfill a broad range of roles in protein function related to conformational plasticity, ligand binding, and sensing/mediating the effects of oxidative stress. A high degree of internal mobility, intrinsic detection sensitivity of the methyl group, and low copy number have made methionine labeling a popular approach for NMR investigation of selectively labeled protein macromolecules. However, selective labeling approaches are subject to more limited information content. In order to optimize the information available from such studies, we have performed DFT...
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08-25-2010 03:51 PM
[NMR paper] Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemica
Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-pnas_full_free.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an...
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08-22-2010 05:08 PM
[NMR paper] The impact of direct refinement against three-bond HN-C alpha H coupling constants on
The impact of direct refinement against three-bond HN-C alpha H coupling constants on protein structure determination by NMR.
Related Articles The impact of direct refinement against three-bond HN-C alpha H coupling constants on protein structure determination by NMR.
J Magn Reson B. 1994 May;104(1):99-103
Authors: Garrett DS, Kuszewski J, Hancock TJ, Lodi PJ, Vuister GW, Gronenborn AM, Clore GM
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08-22-2010 03:33 AM
[NMR paper] The impact of direct refinement against three-bond HN-C alpha H coupling constants on
The impact of direct refinement against three-bond HN-C alpha H coupling constants on protein structure determination by NMR.
Related Articles The impact of direct refinement against three-bond HN-C alpha H coupling constants on protein structure determination by NMR.
J Magn Reson B. 1994 May;104(1):99-103
Authors: Garrett DS, Kuszewski J, Hancock TJ, Lodi PJ, Vuister GW, Gronenborn AM, Clore GM