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13 C‐Detected Through‐Bond Correlation Experiments for Protein Resonance Assignment by Ultra‐Fast MAS Solid‐State NMR
Author(s) -
BarbetMassin Emeline,
Pell Andrew J.,
Knight Michael J.,
Webber Amy L.,
Felli Isabella C.,
Pierattelli Roberta,
Emsley Lyndon,
Lesage Anne,
Pintacuda Guido
Publication year - 2013
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.201201097
Subject(s) - homonuclear molecule , chemistry , magic angle spinning , crystallography , solid state nuclear magnetic resonance , paramagnetism , microcrystalline , resonance (particle physics) , nuclear magnetic resonance spectroscopy , analytical chemistry (journal) , nuclear magnetic resonance , stereochemistry , molecule , atomic physics , physics , organic chemistry , quantum mechanics , chromatography
We present two sequences which combine ( 1 H, 15 N) and ( 15 N, 13 C) selective cross‐polarization steps with an efficient variant of the J ‐based homonuclear transfer scheme, in which a spin‐state‐selective (S 3 E) block is incorporated to improve both resolution and sensitivity in the direct 13 C 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, 153×2 amino acids), in its diamagnetic (“empty”, Zn II ) and paramagnetic (Cu II , Zn II ) states.