STANEK, Jan; ANDREAS, Loren B.; JAUDZEMS, Kristaps; CALA, Diane; LALLI, Daniela; BERTARELLO, Andrea; SCHUBEIS, Tobias; AKOPJANA, Inara; KOTELOVICA, Svetlana; TARS, Kaspars; PICA, Andrea; LEONE, Serena; PICONE, Delia; XU, Zhi-Qiang; DIXON, Nicholas E.; MARTINEZ, Denis; BERBON, Melanie; EL MAMMERI, Nadia; NOUBHANI, Abdelmajid; SAUPE, Sven; HABENSTEIN, Birgit; LOQUET, Antoine; PINTACUDA, Guido

doi:10.1002/anie.201607084

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Angewandte Chemie (International ed. in English). 2016, vol. 55, n° 50, p. 15503-15509

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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 Calpha-Halpha plane is demonstrated for 5 proteins, including microcrystals, a sedimented complex, a capsid and amyloid fibrils. A set of 3D spectra based on a Calpha-Halpha detection block was developed and applied for the sequence-specific backbone and aliphatic side-chain resonance assignment using only 500 mug of sample. These developments accelerate structural studies of biomolecular assemblies available in submilligram quantities without the need of protein deuteration.< Réduire

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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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