Three-dimensional triple-resonance NMR Spectroscopy of isotopically enriched proteins
Three-dimensional triple-resonance NMR Spectroscopy of isotopically enriched proteins
Publication year: 2011
Source: Journal of Magnetic Resonance, Volume 213, Issue 2, December 2011, Pages 423-441</br>
Lewis E.*Kay, Mitsuhiko*Ikura, Rolf*Tschudin, Ad*Bax</br>
Four new and complementary three-dimensional triple-resonance experiments are described for obtaining complete backboneH,C, andN resonance assignments of proteins uniformly enriched withC andN. The new methods all rely onH detection and use multiple magnetization transfers through well-resolved one-bondJcouplings. Therefore, the...
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11-15-2011 10:36 AM
Rapid Solid-State NMR of Deuterated Proteins by Interleaved Cross-Polarization fromH andH Nuclei
Rapid Solid-State NMR of Deuterated Proteins by Interleaved Cross-Polarization fromH andH Nuclei
Publication year: 2011
Source: Journal of Magnetic Resonance, Available online 9 November 2011</br>
Morten*Bjerring, Berit*Paaske, Hartmut*Oschkinat, Umit*Akbey, Niels Chr.*Nielsen</br>
We present a novel sampling strategy, interleaving acquisition of multiple NMR spectra by exploiting initial polarization subsequently fromH andH spins, taking advantage of their differentT1relaxation times. DifferentH- andH-polarization based spectra are in this way simultaneously recorded improving either...
Ergodicity and efficiency of cross-polarization in NMR of static solids.
Ergodicity and efficiency of cross-polarization in NMR of static solids.
Ergodicity and efficiency of cross-polarization in NMR of static solids.
J Magn Reson. 2011 Apr;209(2):161-6
Authors: Nevzorov AA
Cross-polarization transfer is employed in virtually every solid-state NMR experiment to enhance magnetization of low-gamma spins. Theory and experiment is used to assess the magnitude of the final quasistationary magnetization amplitude. The many-body density matrix equation is solved for relatively large (up to N=14) spin systems without the...
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07-23-2011 08:54 AM
Repetitive cross-polarization contacts via equilibration-re-equilibration of the proton bath: sensitivity enhancement for NMR of membrane proteins reconstituted in magnetically aligned bicelles
Repetitive cross-polarization contacts via equilibration-re-equilibration of the proton bath: sensitivity enhancement for NMR of membrane proteins reconstituted in magnetically aligned bicelles
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 2 July 2011</br>
Wenxing, Tang , Alexander A., Nevzorov</br>
Thermodynamic limit of magnetization corresponding to the intact proton bath often cannot be transferred in a single cross-polarization contact. This is mainly due to the finite ratio between the number densities of the high-...
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07-05-2011 05:52 AM
[NMR paper] Sensitive high resolution inverse detection NMR spectroscopy of proteins in the solid
Sensitive high resolution inverse detection NMR spectroscopy of proteins in the solid state.
Related Articles Sensitive high resolution inverse detection NMR spectroscopy of proteins in the solid state.
J Am Chem Soc. 2003 Dec 24;125(51):15831-6
Authors: Paulson EK, Morcombe CR, Gaponenko V, Dancheck B, Byrd RA, Zilm KW
A new indirect detection scheme for obtaining (15)N/(1)H shift correlation spectra in crystalline proteins is described. Excellent water suppression is achieved without the need for pulsed field gradients, and using only a...
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11-24-2010 09:16 PM
[NMR paper] Polarization transfer by cross-correlated relaxation in solution NMR with very large
Polarization transfer by cross-correlated relaxation in solution NMR with very large molecules.
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 Polarization transfer by cross-correlated relaxation in solution NMR with very large molecules.
Proc Natl Acad Sci U S A. 1999 Apr 27;96(9):4918-23
Authors: Riek R, Wider G, Pervushin K, Wüthrich...