Sensitivity enhancement of homonuclear multidimensional NMR correlations for labile sites in proteins, polysaccharides, and nucleic acids.
Nat Commun. 2020 10 21;11(1):5317
Authors: Novakovic M, Kup?e ?, Oxenfarth A, Battistel MD, Freedberg DI, Schwalbe H, Frydman L
Abstract
Multidimensional TOCSY and NOESY are central experiments in chemical and biophysical NMR. Limited efficiencies are an intrinsic downside of these methods, particularly when targeting labile sites. This study demonstrates that the decoherence imparted on these protons through solvent exchanges can, when suitably manipulated, lead to dramatic sensitivity gains per unit time in the acquisition of these experiments. To achieve this, a priori selected frequencies are encoded according to Hadamard recipes, while concurrently subject to looped selective inversion or selective saturation procedures. Suitable processing then leads to protein, oligosaccharide and nucleic acid cross-peak enhancements of ?200-1000% per scan, in measurements that are ?10-fold faster than conventional counterparts. The extent of these gains will depend on the solvent exchange and relaxation rates of the targeted sites; these gains also benefit considerably from the spectral resolution provided by ultrahigh fields, as corroborated by NMR experiments at 600 MHz and 1 GHz. The mechanisms underlying these experiments' enhanced efficiencies are analyzed on the basis of three-way polarization transfer interplays between the water, labile and non-labile protons, and the experimental results are rationalized using both analytical and numerical derivations. Limitations as well as further extensions of the proposed methods, are also discussed.
[NMR paper] Relaxation-compensated difference spin diffusion NMR for detecting (13)C- (13)C long-range correlations in proteins and polysaccharides.
Relaxation-compensated difference spin diffusion NMR for detecting (13)C- (13)C long-range correlations in proteins and polysaccharides.
Relaxation-compensated difference spin diffusion NMR for detecting (13)C- (13)C long-range correlations in proteins and polysaccharides.
J Biomol NMR. 2014 Dec 16;
Authors: Wang T, Williams JK, Schmidt-Rohr K, Hong M
Abstract
The measurement of long-range distances remains a challenge in solid-state NMR structure determination of biological macromolecules. In 2D and 3D correlation spectra of...
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Relaxation-compensated difference spin diffusion NMR for detecting 13 Câ?? 13 C long-range correlations in proteins and polysaccharides
Relaxation-compensated difference spin diffusion NMR for detecting 13 Câ?? 13 C long-range correlations in proteins and polysaccharides
Abstract
The measurement of long-range distances remains a challenge in solid-state NMR structure determination of biological macromolecules. In 2D and 3D correlation spectra of uniformly 13C-labeled biomolecules, inter-residue, inter-segmental, and intermolecular 13Câ??13C cross peaks that provide important long-range distance constraints for three-dimensional structures often overlap with short-range cross peaks...
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[NMR paper] Accurate ab initio prediction of NMR chemical shifts of nucleic acids and nucleic acids/protein complexes.
Accurate ab initio prediction of NMR chemical shifts of nucleic acids and nucleic acids/protein complexes.
Related Articles Accurate ab initio prediction of NMR chemical shifts of nucleic acids and nucleic acids/protein complexes.
Nucleic Acids Res. 2014 Nov 17;
Authors: Victora A, Möller HM, Exner TE
Abstract
NMR chemical shift predictions based on empirical methods are nowadays indispensable tools during resonance assignment and 3D structure calculation of proteins. However, owing to the very limited statistical data basis,...
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11-19-2014 04:32 PM
[NMR paper] Recommendations for the presentation of NMR structures of proteins and nucleic acids-
Recommendations for the presentation of NMR structures of proteins and nucleic acids--IUPAC-IUBMB-IUPAB Inter-Union Task Group on the standardization of data bases of protein and nucleic acid structures determined by NMR spectroscopy.
Related Articles Recommendations for the presentation of NMR structures of proteins and nucleic acids--IUPAC-IUBMB-IUPAB Inter-Union Task Group on the standardization of data bases of protein and nucleic acid structures determined by NMR spectroscopy.
Eur J Biochem. 1998 Aug 15;256(1):1-15
Authors: Markley JL, Bax A, Arata...
Sensitivity enhancement of homonuclear multidimensional NMR correlations for labile sites in proteins, polysaccharides, and nucleic acids.
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