C-13-Detected Through-Bond Correlation Experiments for Protein Resonance Assignment by Ultra-Fast MAS Solid-State NMR

We present two sequences which combine (H-1,N-15) and (N-15,C-13) selective cross-polarization steps with an efficient variant of the J-based homonuclear transfer scheme, in which a spin-state-selective ((SE)-E-3) block is incorporated to improve both resolution and sensitivity in the direct C-13 dimension. We propose these two sequences as a part of a suite of four N-C correlation experiments allowing for the assignment of protein backbone resonances in the solid state. We illustrate these experiments under ultra-fast magic angle spinning conditions on two samples of microcrystalline dimeric human superoxide dismutase (SOD, 153x2 amino acids), in its diamagnetic (empty, Zn-II) and paramagnetic (Cu-II, Zn-II) states.


Published in:
CHEMPHYSCHEM, 14, 13, SI, 3131-3137
Year:
2013
Publisher:
WILEY-V C H VERLAG GMBH
ISSN:
1439-4235
Keywords:
Laboratories:




 Record created 2015-01-08, last modified 2018-03-17


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