Efficient resonance assignment of proteins in MAS NMR by simultaneous intra- and inter-residue 3D correlation spectroscopy
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Author(s)
Daviso, Eugenio
Eddy, Matthew Thomas
Andreas, Loren
Herzfeld, Judith
Griffin, Robert Guy
Date Issued
January 2013
Journal
Journal of Biomolecular NMR
Publisher
Springer-Verlag
Citation
Daviso, Eugenio, Matthew T. Eddy, Loren B. Andreas, Robert G. Griffin, and Judith Herzfeld. “Efficient Resonance Assignment of Proteins in MAS NMR by Simultaneous Intra- and Inter-Residue 3D Correlation Spectroscopy.” Journal of Biomolecular NMR 55, no. 3 (January 19, 2013): 257–265.
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Author's final manuscript
Abstract
Resonance assignment is the first step in NMR structure determination. For magic angle spinning NMR, this is typically achieved with a set of heteronuclear correlation experiments (NCaCX, NCOCX, CONCa) that utilize SPECIFIC-CP [superscript 15]N–[superscript 13]C transfers. However, the SPECIFIC-CP transfer efficiency is often compromised by molecular dynamics and probe performance. Here we show that one-bond ZF-TEDOR [superscript 15]N– [superscript 13]C transfers provide simultaneous NCO and NCa correlations with at least as much sensitivity as SPECIFIC-CP for some non-crystalline samples. Furthermore, a 3D ZF-TEDOR-CC experiment provides heteronuclear sidechain correlations and robustness with respect to proton decoupling and radiofrequency power instabilities. We demonstrate transfer efficiencies and connectivities by application of 3D ZF-TEDOR-DARR to a model microcrystalline protein, GB1, and a less ideal system, GvpA in intact gas vesicles.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
Francis Bitter Magnet Laboratory (Massachusetts Institute of Technology)
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DOI of Published Version
http://dx.doi.org/10.1007/s10858-013-9707-0
