Title

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

RIS ID

111109

Publication Details

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., Dixon, N. E., Martinez, D., Berbon, M., El Mammeri, N., Noubhani, A., Saupe, S., Habenstein, B., Loquet, A. & Pintacuda, G. (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), 15504-15509.

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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Link to publisher version (DOI)

http://dx.doi.org/10.1002/anie.201607084