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NMR Spectroscopic Assignment of Backbone and Side‐Chain Protons in Fully Protonated Proteins: Microcrystals, Sedimented Assemblies, and Amyloid Fibrils
Author(s) -
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 ZhiQiang,
Dixon Nicholas E.,
Martinez Denis,
Berbon Mélanie,
El Mammeri Nadia,
Noubhani Abdelmajid,
Saupe Sven,
Habenstein Birgit,
Loquet Antoine,
Pintacuda Guido
Publication year - 2016
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201607084
Subject(s) - side chain , protonation , magic angle spinning , crystallography , chemistry , nuclear magnetic resonance spectroscopy , solid state nuclear magnetic resonance , fibril , amyloid fibril , spectroscopy , stereochemistry , amyloid β , nuclear magnetic resonance , ion , polymer , organic chemistry , physics , biochemistry , medicine , disease , pathology , quantum mechanics
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.