Protein residue linking in a single spectrum for magic-angle spinning NMR 
assignment.

Andreas, L. B.; Stanek, J.; Le Marchand, T.; Bertarello, A.; Paepe, D. C. D.; Lalli, D.; Krejcikova, M.; Doyen, C.; Oster, C.; Knott, B.; Wegner, S.; Engelke, F.; Felli, I. C.; Pierattelli, R.; Dixon, N. E.; Emsley, L.; Herrmann, T.; Pintacuda, G.

doi:10.1007/s10858-015-9956-1

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Protein residue linking in a single spectrum for magic-angle spinning NMR assignment.

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Andreas, L. B.
Research Group of Solid State NMR Spectroscopy-2, MPI for Biophysical Chemistry, Max Planck Society;

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Citation

Andreas, L. B., Stanek, J., Le Marchand, T., Bertarello, A., Paepe, D. C. D., Lalli, D., et al. (2015). Protein residue linking in a single spectrum for magic-angle spinning NMR assignment. Journal of Biomolecular NMR, 62(3), 253-261. doi:10.1007/s10858-015-9956-1.

Cite as: https://hdl.handle.net/11858/00-001M-0000-002E-9233-C

Abstract

Here we introduce a new pulse sequence for resonance assignment that halves the number of data sets required for sequential linking by directly correlating sequential amide resonances in a single diagonal-free spectrum. The method is demonstrated with both microcrystalline and sedimented deuterated proteins spinning at 60 and 111 kHz, and a fully protonated microcrystalline protein spinning at 111 kHz, with as little as 0.5 mg protein sample. We find that amide signals have a low chance of ambiguous linkage, which is further improved by linking in both forward and backward directions. The spectra obtained are amenable to automated resonance assignment using general-purpose software such as UNIO-MATCH.