Bacteriophage Tail Tube Assembly Studied by Proton-Detected 4D Solid-State NMR.
 

Bacteriophage Tail Tube Assembly Studied by Proton-Detected 4D Solid-State NMR.

Related Articles Bacteriophage Tail Tube Assembly Studied by Proton-Detected 4D Solid-State NMR.

Angew Chem Int Ed Engl. 2017 Jun 23;:

Authors: Zinke M, Fricke P, Samson C, Hwang S, Wall J, Lange S, Zinn-Justin S, Lange A

Abstract
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.


PMID: 28644511 [PubMed - as supplied by publisher]



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