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.; Schubeis, T.; Akopjana, I.; Kotelovica, S.; Tars, K.; Pica, A.; Leone, S.; Picone, D.; Xu, Z. Q.; Dixon, N. E.; Martinez, D.; Berbon, M.; El Mammeri, N.; Noubhani, A.; Saupe, S.; Habenstein, B.; Loquet, A,; Pintacuda, G.

doi:10.1002/anie.201607084

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

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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

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.

Cite as: https://hdl.handle.net/11858/00-001M-0000-002E-91EB-5

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.