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  4. Backbone Assignment of Fully Protonated Solid Proteins by 1H Detection and Ultrafast Magic-Angle-Spinning NMR Spectroscopy
 
research article

Backbone Assignment of Fully Protonated Solid Proteins by 1H Detection and Ultrafast Magic-Angle-Spinning NMR Spectroscopy

Marchetti, Alessandro
•
Jehle, Stefan
•
Felletti, Michele
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2012
Angewandte Chemie International Edition

Narrow 1H NMR linewidths can be obtained for fully protonated protein samples in the solid state by using ultrafast magic-angle spinning (60 kHz). Medium-size microcrystalline and noncrystalline proteins can be analyzed without any need for deuteration of the protein sample. This approach provides assignments of the backbone 1H, 15N, 13C α, and 13CO resonances and yields information about 1H-1H proximities. Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

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Type
research article
DOI
10.1002/anie.201203124
Web of Science ID

WOS:000310076100012

Author(s)
Marchetti, Alessandro
Jehle, Stefan
Felletti, Michele
Knight, Michael J.
Wang, Yao
Xu, Zhi-Qiang
Park, Ah Young
Otting, Gottfried
Lesage, Anne
Emsley, Lyndon  
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Date Issued

2012

Publisher

Wiley-VCH Verlag GmbH

Published in
Angewandte Chemie International Edition
Volume

51

Issue

43

Start page

10756

End page

10759

Subjects

DNA polymerase

•

magic-angle spinning

•

NMR spectroscopy

•

protein structures

•

scalar transfers

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/20.500.14299/109993
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