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- Title
NMR Spectroscopic Assignment of Backbone and Side-Chain Protons in Fully Protonated Proteins: Microcrystals, Sedimented Assemblies, and Amyloid Fibrils.
- Authors
Stanek, Jan; Andreas, Loren B.; Jaudzems, Kristaps; Cala, Diane; Lalli, Daniela; Bertarello, Andrea; Schubeis, Tobias; Pintacuda, Guido; Akopjana, Inara; Kotelovica, Svetlana; Tars, Kaspars; Pica, Andrea; Leone, Serena; Picone, Delia; Xu, Zhi-Qiang; Dixon, Nicholas E.; Martinez, Denis; Berbon, Mélanie; El Mammeri, Nadia; Noubhani, Abdelmajid
- 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.
- Subjects
NUCLEAR magnetic resonance; PROTONS; MAGIC angle spinning; DEUTERATION; HETERONUCLEAR diatomic molecules
- Publication
Angewandte Chemie International Edition, 2016, Vol 55, Issue 50, p15504
- ISSN
1433-7851
- Publication type
Article
- DOI
10.1002/anie.201607084