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Frontispiece: 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 - Reports
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201685061
Subject(s) - magic angle spinning , side chain , crystallography , amyloid fibril , protonation , solid state nuclear magnetic resonance , high resolution , fibril , materials science , nuclear magnetic resonance spectroscopy , chemistry , nuclear magnetic resonance , stereochemistry , amyloid β , polymer , physics , organic chemistry , medicine , ion , biochemistry , disease , pathology , remote sensing , composite material , geology
Protein Structures G. Pintacuda et al. show in their Communication on page 15504 ff. that with 111 kHz magic‐angle spinning probes, high‐resolution 1 H‐detected solid‐state NMR spectra of proteins can be acquired without deuteration.