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  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., 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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-9233-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-9237-4
Genre: Journal Article

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2517743.pdf (Publisher version), 2MB
 
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 Creators:
Andreas, L. B.1, Author              
Stanek, J., Author
Le Marchand, T., Author
Bertarello, A., Author
Paepe, D. C. D., Author
Lalli, D., Author
Krejcikova, M., Author
Doyen, C., Author
Oster, C., Author
Knott, B., Author
Wegner, S., Author
Engelke, F., Author
Felli, I. C., Author
Pierattelli, R., Author
Dixon, N. E., Author
Emsley, L., Author
Herrmann, T., Author
Pintacuda, G., Author
Affiliations:
1Research Group of Solid State NMR Spectroscopy-2, MPI for Biophysical Chemistry, Max Planck Society, ou_2396693              

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Free keywords: Magic-angle spinning; Protein resonance assignment; Proton detection; Automation
 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.

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Language(s): eng - English
 Dates: 2017-06-162015-07
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1007/s10858-015-9956-1
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Title: Journal of Biomolecular NMR
Source Genre: Journal
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Pages: - Volume / Issue: 62 (3) Sequence Number: - Start / End Page: 253 - 261 Identifier: -