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  NMR spectroscopic assignment of backbone and side-chain protons in fully protonated proteins: Microcrystals, sedimented assemblies, and amyloid fibrils.

Stanek, J., Andreas, L. B., Jaudzems, K., Cala, D., Lalli, D., Bertarello, A., et al. (2016). NMR spectroscopic assignment of backbone and side-chain protons in fully protonated proteins: Microcrystals, sedimented assemblies, and amyloid fibrils. Angewandte Chemie International Edition, 55(50), 15504-155509. doi:10.1002/anie.201607084.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-91EB-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-91EF-E
Genre: Journal Article

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 Creators:
Stanek, J., Author
Andreas, L. B.1, Author              
Jaudzems, K., Author
Cala, D., Author
Lalli, D., Author
Bertarello, A., Author
Schubeis, T., Author
Akopjana, I., Author
Kotelovica, S., Author
Tars, K., Author
Pica, A., Author
Leone, S., Author
Picone, D., Author
Xu, Z. Q., Author
Dixon, N. E., Author
Martinez, D., Author
Berbon, M., Author
El Mammeri, N., Author
Noubhani, A., Author
Saupe, S., Author
Habenstein, B., AuthorLoquet, A,, AuthorPintacuda, G., Author more..
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; proton detection; resonance assignment; solid-state NMR spectroscopy
 Abstract: We demonstrate sensitive detection of alpha protons of fully protonated proteins by solid-state NMR spectroscopy with 100–111 kHz magic-angle spinning (MAS). The excellent resolution in the Cα-Hα plane is demonstrated for 5 proteins, including microcrystals, a sedimented complex, a capsid and amyloid fibrils. A set of 3D spectra based on a Cα–Hα detection block was developed and applied for the sequence-specific backbone and aliphatic side-chain resonance assignment using only 500 μg of sample. These developments accelerate structural studies of biomolecular assemblies available in submilligram quantities without the need of protein deuteration.

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Language(s): eng - English
 Dates: 2016-11-162016-12-12
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1002/anie.201607084
 Degree: -

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Title: Angewandte Chemie International Edition
Source Genre: Journal
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Pages: - Volume / Issue: 55 (50) Sequence Number: - Start / End Page: 15504 - 155509 Identifier: -