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  Structure of fully protonated proteins by proton-detected magic-angle spinning NMR.

Andreas, L. B., Jaudzems, K., Stanek, J., Lalli, D., Bertarello, A., Le Marchand, T., et al. (2016). Structure of fully protonated proteins by proton-detected magic-angle spinning NMR. Proceedings of the National Academy of Sciences of the United States of America, 113(33), 9187-9192. doi:10.1073/pnas.1602248113.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-9201-B Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-9206-1
Genre: Journal Article

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 Creators:
Andreas, L. B.1, Author              
Jaudzems, K., Author
Stanek, J., Author
Lalli, D., Author
Bertarello, A., Author
Le Marchand, T., Author
Paepe, D. C. D., Author
Kotelovica, S., Author
Akopjana, I., Author
Knott, B., Author
Wegner, S., Author
Engelke, F., Author
Lesage, A., Author
Emsley, L., Author
Tars, K., 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: NMR spectroscopy; magic-angle spinning; protein structures; proton detection; viral nucleocapsids
 Abstract: Protein structure determination by proton-detected magic-angle spinning (MAS) NMR has focused on highly deuterated samples, in which only a small number of protons are introduced and observation of signals from side chains is extremely limited. Here, we show in two fully protonated proteins that, at 100-kHz MAS and above, spectral resolution is high enough to detect resolved correlations from amide and side-chain protons of all residue types, and to reliably measure a dense network of 1H-1H proximities that define a protein structure. The high data quality allowed the correct identification of internuclear distance restraints encoded in 3D spectra with automated data analysis, resulting in accurate, unbiased, and fast structure determination. Additionally, we find that narrower proton resonance lines, longer coherence lifetimes, and improved magnetization transfer offset the reduced sample size at 100-kHz spinning and above. Less than 2 weeks of experiment time and a single 0.5-mg sample was sufficient for the acquisition of all data necessary for backbone and side-chain resonance assignment and unsupervised structure determination. We expect the technique to pave the way for atomic-resolution structure analysis applicable to a wide range of proteins.

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Language(s): eng - English
 Dates: 2016-08-16
 Publication Status: Published online
 Pages: -
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1073/pnas.1602248113
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Title: Proceedings of the National Academy of Sciences of the United States of America
Source Genre: Journal
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Pages: - Volume / Issue: 113 (33) Sequence Number: - Start / End Page: 9187 - 9192 Identifier: -