[NMR paper] Bidirectional band-selective magnetization transfer along the protein backbone doubles the information content of solid-state NMR correlation experiments.
Bidirectional band-selective magnetization transfer along the protein backbone doubles the information content of solid-state NMR correlation experiments.
Related ArticlesBidirectional band-selective magnetization transfer along the protein backbone doubles the information content of solid-state NMR correlation experiments.
J Biomol NMR. 2017 Nov 08;:
Authors: Jolly MM, Jarvis JA, Carravetta M, Levitt MH, Williamson PTF
Abstract
Resonance assignment is the first stage towards solving the structure of a protein. This is normally achieved by the employment of separate inter and intra residue experiments. By utilising the mixed rotation and rotary recoupling (MIRROR) condition it is possible to double the information content through the efficient bidirectional transfer of magnetization from the CO to its adjacent C? and the C? of the subsequent amino acid. We have incorporated this into a 3D experiment, a 3D-MIRROR-NCOCA, where correlations present in the 3D spectrum permit the sequential assignment of the protein backbone from a single experiment as we have demonstrated on a microcrystalline preparation of GB3. Furthermore, the low-power requirements of the MIRROR recoupling sequence facilitate the development of a low-power 3D-NCOCA experiment. This has enabled us to realise significant reductions in acquisition times, allowing the acquisition of a single 3D-NCOCA spectrum suitable for a full backbone resonance assignment of GB3 in less than 24*h.
PMID: 29116557 [PubMed - as supplied by publisher]
Bidirectional band-selective magnetization transfer along the protein backbone doubles the information content of solid-state NMR correlation experiments
Bidirectional band-selective magnetization transfer along the protein backbone doubles the information content of solid-state NMR correlation experiments
Abstract
Resonance assignment is the first stage towards solving the structure of a protein. This is normally achieved by the employment of separate inter and intra residue experiments. By utilising the mixed rotation and rotary recoupling (MIRROR) condition it is possible to double the information content through the efficient bidirectional transfer of magnetization from the CO to its adjacent Cα...
[NMR paper] Long-Observation-Window Band-Selective Homonuclear Decoupling: Increased Sensitivity and Resolution in Solid-State NMR Spectroscopy of Proteins
Long-Observation-Window Band-Selective Homonuclear Decoupling: Increased Sensitivity and Resolution in Solid-State NMR Spectroscopy of Proteins
Publication date: Available online 13 September 2013
Source:Journal of Magnetic Resonance</br>
Author(s): Jochem O. Struppe , Chen Yang , Yachong Wang , Roy V. Hernandez , Lisa M. Shamansky , Leonard J. Mueller</br>
Sensitivity and resolution are the two fundamental obstacles to extending solid-state nuclear magnetic resonance to even larger protein systems. Here, a novel long-observation-window band-selective...
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[NMR paper] (13) C-Detected Through-Bond Correlation Experiments for Protein Resonance Assignment by Ultra-Fast MAS Solid-State NMR.
(13) C-Detected Through-Bond Correlation Experiments for Protein Resonance Assignment by Ultra-Fast MAS Solid-State NMR.
Related Articles (13) C-Detected Through-Bond Correlation Experiments for Protein Resonance Assignment by Ultra-Fast MAS Solid-State NMR.
Chemphyschem. 2013 Apr 15;
Authors: Barbet-Massin E, Pell AJ, Knight MJ, Webber AL, Felli IC, Pierattelli R, Emsley L, Lesage A, Pintacuda G
Abstract
We present two sequences which combine ((1) H,(15) N) and ((15) N,(13) C) selective cross-polarization steps with an efficient variant...
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04-17-2013 08:15 PM
[NMR paper] Efficient CO-CA transfer in highly deuterated proteins by band-selective homonuclear cross-polarization
Efficient CO-CA transfer in highly deuterated proteins by band-selective homonuclear cross-polarization
Available online 14 March 2013
Publication year: 2013
Source:Journal of Magnetic Resonance</br>
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Robust and efficient band-selective magnetization transfer between CO and CA spins can be achieved in highly deuterated solid proteins by dipolar-based homonuclear cross polarization. The approach is designed for moderate magic-angle spinning rates and high external magnetic fields where the isotropic chemical shift difference of CO and CA considerably exceeds the...
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Dual-band Selective Double Cross Polarization for Heteronuclear Polarization Transfer between Dilute Spins in Solid-State MAS NMR
Dual-band Selective Double Cross Polarization for Heteronuclear Polarization Transfer between Dilute Spins in Solid-State MAS NMR
Publication year: 2012
Source:Journal of Magnetic Resonance</br>
Zhengfeng Zhang, Yimin Miao, Xiaoli Liu, Jun Yang, Conggang Li, Feng Deng, Riqiang Fu</br>
A sinusoidal modulation scheme is described for selective heteronuclear polarization transfer between two dilute spins in double cross polarization magic-angle-spinning nuclear magnetic resonance spectroscopy. During the second N->C cross polarization, the 13C RF amplitude is...
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03-09-2012 09:16 AM
Dual-band Selective Double Cross Polarization for Heteronuclear Polarization Transfer between Dilute Spins in Solid-State MAS NMR
Dual-band Selective Double Cross Polarization for Heteronuclear Polarization Transfer between Dilute Spins in Solid-State MAS NMR
Publication year: 2012
Source: Journal of Magnetic Resonance, Available online 5 March 2012</br>
Zhengfeng*Zhang, Yimin*Miao, Xiaoli*Liu, Jun*Yang, Conggang*Li, ...</br>
A sinusoidal modulation scheme is described for selective heteronuclear polarization transfer between two dilute spins in double cross polarization magic-angle-spinning nuclear magnetic resonance spectroscopy. During the second N->C cross polarization, theC RF amplitude is modulated...
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[NMR paper] Dissection of heteronuclear NMR experiments for studies of magnetization transfer eff
Dissection of heteronuclear NMR experiments for studies of magnetization transfer efficiencies.
Related Articles Dissection of heteronuclear NMR experiments for studies of magnetization transfer efficiencies.
J Magn Reson. 2003 Nov;165(1):89-94
Authors: Braun D, Wüthrich K, Wider G
Modern NMR experiments for applications with biological macromolecules in solution typically include multiple magnetization transfer steps. When working with large structures, a significant fraction of the magnetization is lost during these transfers. For the design...
Bidirectional band-selective magnetization transfer along the protein backbone doubles the information content of solid-state NMR correlation experiments.
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