Related ArticlesMultidimensional triple resonance NMR spectroscopy of isotopically uniformly enriched proteins: a powerful new strategy for structure determination.
Ciba Found Symp. 1991;161:108-19; discussion 119-35
Authors: Bax A, Ikura M, Kay LE, Barbato G, Spera S
A procedure is described that affords complete 1H, 13C and 15N resonance assignment in proteins of up to about 25 kDa. The new approach requires uniform isotopic enrichment of the protein with 13C and 15N and correlates resonances of adjacent nuclei using the relatively large and well-resolved one-bond J couplings. Spectral overlap, a common problem in the application of two-dimensional NMR, is removed by increasing the dimensionality of the new methods to three or four, without increasing the number of observed resonances. With complete 1H, 13C and 15N resonance assignments available, the nuclear Overhauser effect (NOE)-based interproton distance constraints can be extracted in a very straightforward manner from four-dimensional NOE spectra.
Application of iterative soft thresholding for fast reconstruction of NMR data non-uniformly sampled with multidimensional Poisson Gap scheduling
Application of iterative soft thresholding for fast reconstruction of NMR data non-uniformly sampled with multidimensional Poisson Gap scheduling
Abstract The fast Fourier transformation has been the gold standard for transforming data from time to frequency domain in many spectroscopic methods, including NMR. While reliable, it has as a drawback that it requires a grid of uniformly sampled data points. This needs very long measuring times for sampling in multidimensional experiments in all indirect dimensions uniformly and even does not allow reaching optimal evolution times that would...
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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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12-11-2011 07:57 AM
Mammalian production of an isotopically enriched outer domain of the HIV-1 gp120 glycoprotein for NMR spectroscopy.
Mammalian production of an isotopically enriched outer domain of the HIV-1 gp120 glycoprotein for NMR spectroscopy.
Mammalian production of an isotopically enriched outer domain of the HIV-1 gp120 glycoprotein for NMR spectroscopy.
J Biomol NMR. 2011 Jun 12;
Authors: Sastry M, Xu L, Georgiev IS, Bewley CA, Nabel GJ, Kwong PD
NMR spectroscopic characterization of the structure or the dynamics of proteins generally requires the production of samples isotopically enriched in (15)N, (13)C, or (2)H. The bacterial expression systems currently in use to...
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06-15-2011 01:15 PM
Mammalian production of an isotopically enriched outer domain of the HIV-1 gp120 glycoprotein for NMR spectroscopy
Mammalian production of an isotopically enriched outer domain of the HIV-1 gp120 glycoprotein for NMR spectroscopy
Abstract NMR spectroscopic characterization of the structure or the dynamics of proteins generally requires the production of samples isotopically enriched in 15N, 13C, or 2H. The bacterial expression systems currently in use to obtain isotopic enrichment, however, cannot produce a number of eukaryotic proteins, especially those that require post-translational modifications such as N-linked glycosylation for proper folding or activity. Here, we report the use of an...
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06-15-2011 02:31 AM
First solid-state NMR analysis of uniformly (13)C-enriched major light-harvesting complexes from Chlamydomonas reinhardtti and identification of protein and cofactor spin clusters.
First solid-state NMR analysis of uniformly (13)C-enriched major light-harvesting complexes from Chlamydomonas reinhardtti and identification of protein and cofactor spin clusters.
First solid-state NMR analysis of uniformly (13)C-enriched major light-harvesting complexes from Chlamydomonas reinhardtti and identification of protein and cofactor spin clusters.
Biochim Biophys Acta. 2011 Jan 25;
Authors: Pandit A, Morosinotto T, Reus M, Holzwarth AR, Bassi R, de Groot HJ
The light-harvesting complex II (LHCII) is the main component of the...
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02-02-2011 02:40 AM
[NMR paper] Partial NMR assignments for uniformly (13C, 15N)-enriched BPTI in the solid state.
Partial NMR assignments for uniformly (13C, 15N)-enriched BPTI in the solid state.
Related Articles Partial NMR assignments for uniformly (13C, 15N)-enriched BPTI in the solid state.
J Biomol NMR. 2000 Mar;16(3):209-19
Authors: McDermott A, Polenova T, Bockmann A, Zilm KW, Paulson EK, Martin RW, Montelione GT, Paulsen EK
We demonstrate that high-resolution multidimensional solid state NMR methods can be used to correlate many backbone and side chain chemical shifts for hydrated micro-crystalline U-13C,15N Basic Pancreatic Trypsin Inhibitor...
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11-18-2010 09:15 PM
[NMR paper] Triple-resonance multidimensional NMR study of calmodulin complexed with the binding
Triple-resonance multidimensional NMR study of calmodulin complexed with the binding domain of skeletal muscle myosin light-chain kinase: indication of a conformational change in the central helix.
Related Articles Triple-resonance multidimensional NMR study of calmodulin complexed with the binding domain of skeletal muscle myosin light-chain kinase: indication of a conformational change in the central helix.
Biochemistry. 1991 Jun 4;30(22):5498-504
Authors: Ikura M, Kay LE, Krinks M, Bax A
Heteronuclear 3D and 4D NMR experiments have been...
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08-21-2010 11:16 PM
[NMR paper] Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1 bet
Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1 beta in solution.
Related Articles Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1 beta in solution.
Science. 1990 Jul 27;249(4967):411-4
Authors: Kay LE, Clore GM, Bax A, Gronenborn AM
A method is presented that dramatically improves the resolution of protein nuclear magnetic resonance (NMR) spectra by increasing their dimensionality to four. The power of this technique is demonstrated by the application of four-dimensional...
Multidimensional triple resonance NMR spectroscopy of isotopically uniformly enriched
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