Protein oligomers studied by solid-state NMR – the case of the full-length nucleoid-associated protein histone-like nucleoid structuring protein
Article first published online: 13 MAY 2013
© 2013 FEBS
Volume 280, Issue 12, pages 2916–2928, June 2013
How to Cite
Renault, M., García, J., Cordeiro, T. N., Baldus, M. and Pons, M. (2013), Protein oligomers studied by solid-state NMR – the case of the full-length nucleoid-associated protein histone-like nucleoid structuring protein. FEBS Journal, 280: 2916–2928. doi: 10.1111/febs.12297
- Issue published online: 6 JUN 2013
- Article first published online: 13 MAY 2013
- Accepted manuscript online: 19 APR 2013 11:50PM EST
- Manuscript Accepted: 16 APR 2013
- Manuscript Revised: 3 APR 2013
- Manuscript Received: 18 NOV 2012
- European Community's Seventh Framework Programme
- European Community's Seventh Framework Programme. Grant Numbers: FP7/2007–2013, 211800, 261863
- Spanish Ministry of Science and Innovation-FEDER. Grant Number: BIO2010-15683
- NWO. Grant Numbers: 700.26.121, 700.58.102
- Generalitat de Catalunya. Grant Number: 2009SGR1352
Table S1. Solid-state NMR chemical shifts of self-assembled (U-13C,15N)-labeled full-length H-NS.
Table S2. Solid-state NMR chemical shifts of (U-13C,15N) H-NS 1–47.
Table S3. 1H, 13C and 15N solution NMR chemical shifts of (U-13C,15N) H-NS 1–47.
Fig. S1. 2D NCOCX correlation spectrum obtained on (U-13C,15N)-labeled full-length H-NS.
Fig. S2. Overlay of the 2D 13C–13C correlation spectra obtained on (U-13C,15N)-labeled full-length H-NS and its truncated variant H-NS 1–47.
Fig. S3. Histogram representation of Cα secondary chemical shifts and chemical shift differences between H-NS 1–47 in solid state and in solution and solid-state H-NS 1–137.
Fig. S4. Functional assays on full-length H-NS samples.
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