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Enhanced resolution and coherence lifetimes in the solid-state NMR spectroscopy of perdeuterated proteins under ultrafast magic-angle spinning

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Lewandowski, Józef R., Dumez, Jean-Nicolas, Akbey, Ümit, Lange, Sascha, Emsley, Lyndon and Oschkinat, Hartmut (2011) Enhanced resolution and coherence lifetimes in the solid-state NMR spectroscopy of perdeuterated proteins under ultrafast magic-angle spinning. Journal of Physical Chemistry Letters, Vol.2 (No.17). pp. 2205-2211. doi:10.1021/jz200844n ISSN 1948-7185.

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Official URL: http://dx.doi.org/10.1021/jz200844n

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Abstract

We investigate the combined effect of perdeuteration and fast magic-angle spinning on the resolution and sensitivity of proton-detected protein NMR spectra and on coherence lifetimes. With 60 kHz spinning of a microcrystalline alpha-spectrin SH3 sample at a field strength of 23 T, a regime is attained where there is no substantial difference in resolution between perdeuterated samples with 10 or 100% protons at the exchangeable sites. (1)H resolution is then limited by inhomogeneous contributions. Upon fast spinning, the most dramatic line narrowing effects are observed for residues in the loop or bend regions of the protein, probably due to the removal of destructive dynamics effects. This investigation paves the way for using samples with 100% protons at the exchangeable sites in structure determination protocols, since all backbone amide sites can now contribute to the signal.

Item Type: Journal Article
Subjects: Q Science > QD Chemistry
Divisions: Faculty of Science, Engineering and Medicine > Science > Chemistry
Library of Congress Subject Headings (LCSH): Nuclear magnetic resonance spectroscopy, Solid state chemistry, Proteins -- Analysis
Journal or Publication Title: Journal of Physical Chemistry Letters
Publisher: American Chemical Society
ISSN: 1948-7185
Official Date: 1 September 2011
Dates:
DateEvent
1 September 2011Published
Volume: Vol.2
Number: No.17
Page Range: pp. 2205-2211
DOI: 10.1021/jz200844n
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access
Funder: France. Agence nationale de la recherche (ANR), Deutsche Forschungsgemeinschaft (DFG), European Union (EU), Seventh Framework Programme (European Commission) (FP7)
Grant number: SFB 740 (DFG), PIRG03-GA-2008-231026 (EU), BioNMR 261863 (FP7), PIRG03-GA-2008-231026 (EU)

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