NMR Spectroscopic Assignment of Backbone and Side-Chain Protons in Fully Protonated Proteins: Microcrystals, Sedimented Assemblies, and Amyloid Fibrils
Language
en
Article de revue
This item was published in
Angewandte Chemie (International ed. in English). 2016, vol. 55, n° 50, p. 15503-15509
English 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 Calpha-Halpha plane is demonstrated ...Read more >
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.Read less <