ArticleJournal of biomolecular NMR2010
GFT projection NMR spectroscopy for proteins in the solid state.
Article in Journal of biomolecular NMR, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Facing and Overcoming Sensitivity Challenges in Biomolecular NMR Spectroscopy.Angewandte Chemie (International ed. in English) · 2015Review
- MAS NMR of HIV-1 protein assemblies.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015Article
- Magic angle spinning NMR of viruses.Progress in nuclear magnetic resonance spectroscopy · 2015Review
- Towards automatic protein backbone assignment using proton-detected 4D solid-state NMR data.Journal of biomolecular NMR · 2014Article
- Sensitivity gains, linearity, and spectral reproducibility in nonuniformly sampled multidimensional MAS NMR spectra of high dynamic range.Journal of biomolecular NMR · 2014Article
- A time-saving strategy for MAS NMR spectroscopy by combining nonuniform sampling and paramagnetic relaxation assisted condensed data collection.The journal of physical chemistry. B · 2012Article
- Enhanced sensitivity by nonuniform sampling enables multidimensional MAS NMR spectroscopy of protein assemblies.The journal of physical chemistry. B · 2012Article
- Simultaneous acquisition of PAR and PAIN spectra.Journal of biomolecular NMR · 2012Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Recording of four-dimensional (4D) spectra for proteins in the solid state has opened new avenues to obtain virtually complete resonance assignments and three-dimensional (3D) structures of proteins. As in solution state NMR, the sampling of three indirect dimensions leads per se to long minimal measurement time. Furthermore, artifact suppression in solid state NMR relies primarily on radio-frequency pulse phase cycling. For an n-step phase cycle, the minimal measurement times of both 3D and 4D spectra are increased n times. To tackle the associated 'sampling problem' and to avoid sampling limited data acquisition, solid state G-Matrix Fourier Transform (SS GFT) projection NMR is introduced to rapidly acquire 3D and 4D spectral information. Specifically, (4,3)D (HA)CANCOCX and (3,2)D (HACA)NCOCX were implemented and recorded for the 6 kDa protein GB1 within about 10% of the time required for acquiring the conventional congeners with the same maximal evolution times and spectral widths in the indirect dimensions. Spectral analysis was complemented by comparative analysis of expected spectral congestion in conventional and GFT NMR experiments, demonstrating that high spectral resolution of the GFT NMR experiments enables one to efficiently obtain nearly complete resonance assignments even for large proteins.
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Registered trials
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