Backbone and side-chain proton NMR assignment in fully protonated proteins: microcrystals, sedimented assemblies, and amyloid fibrils

Abstract : We demonstrate sensitive detection of alpha protons of fully protonated proteins by solid-state NMR 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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Jan Stanek, Loren Andreas, Kristaps Jaudzems, Diane Cala, Daniela Lalli, et al.. Backbone and side-chain proton NMR assignment in fully protonated proteins: microcrystals, sedimented assemblies, and amyloid fibrils. Angewandte Chemie International Edition, Wiley-VCH Verlag, 2016, 55 (50), pp.15504-15509. ⟨http://onlinelibrary.wiley.com/⟩. ⟨10.1002/anie.201607084⟩. ⟨hal-01567784⟩

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