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

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

Barbet-Massin, Emeline
•
Pell, Andrew J.
•
Knight, Michael J.
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2013
CHEMPHYSCHEM

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.

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Type
research article
DOI
10.1002/cphc.201201097
Web of Science ID

WOS:000324316000035

Author(s)
Barbet-Massin, Emeline
Pell, Andrew J.
Knight, Michael J.
Webber, Amy L.
Felli, Isabella C.
Pierattelli, Roberta
Emsley, Lyndon  
Lesage, Anne
Pintacuda, Guido
Date Issued

2013

Publisher

WILEY-V C H VERLAG GMBH

Published in
CHEMPHYSCHEM
Volume

14

Issue

13, SI

Start page

3131

End page

3137

Subjects

J-coupling

•

paramagnetism

•

solid-state nuclear magnetic resonance spectroscopy

•

superoxide dismutase

•

magic angle spinning

Editorial or Peer reviewed

REVIEWED

Written at

OTHER

EPFL units
LRM  
Available on Infoscience
January 8, 2015
Use this identifier to reference this record
https://infoscience.epfl.ch/handle/20.500.14299/109967
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