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Bacteriophage Tail‐Tube Assembly Studied by Proton‐Detected 4D Solid‐State NMR
Author(s) -
Zinke Maximilian,
Fricke Pascal,
Samson Camille,
Hwang Songhwan,
Wall Joseph S.,
Lange Sascha,
ZinnJustin Sophie,
Lange Adam
Publication year - 2017
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201706060
Subject(s) - spectral line , chemistry , supramolecular chemistry , proton , nmr spectra database , solid state nuclear magnetic resonance , carbon 13 nmr satellite , bottleneck , resonance (particle physics) , chemical physics , analytical chemistry (journal) , crystallography , nuclear magnetic resonance , molecule , atomic physics , physics , computer science , organic chemistry , nuclear physics , astronomy , embedded system
Obtaining unambiguous resonance assignments remains a major bottleneck in solid‐state NMR studies of protein structure and dynamics. Particularly for supramolecular assemblies with large subunits (>150 residues), the analysis of crowded spectral data presents a challenge, even if three‐dimensional (3D) spectra are used. Here, we present a proton‐detected 4D solid‐state NMR assignment procedure that is tailored for large assemblies. The key to recording 4D spectra with three indirect carbon or nitrogen dimensions with their inherently large chemical shift dispersion lies in the use of sparse non‐uniform sampling (as low as 2 %). As a proof of principle, we acquired 4D (H)COCANH, (H)CACONH, and (H)CBCANH spectra of the 20 kDa bacteriophage tail‐tube protein gp17.1 in a total time of two and a half weeks. These spectra were sufficient to obtain complete resonance assignments in a straightforward manner without use of previous solution NMR data.