Bacteriophage Tail‐Tube Assembly Studied by Proton‐Detected 4D Solid‐State NMR
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.
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Bibliographic citation
-
Bacteriophage Tail‐Tube Assembly Studied by Proton‐Detected 4D Solid‐State NMR ; volume:129 ; number:32 ; year:2017 ; pages:9625-9629 ; extent:5
Angewandte Chemie ; 129, Heft 32 (2017), 9625-9629 (gesamt 5)
- Creator
-
Zinke, Maximilian
Fricke, Pascal
Samson, Camille
Hwang, Songhwan
Wall, Joseph S.
Lange, Sascha
Zinn‐Justin, Sophie
Lange, Adam
- DOI
-
10.1002/ange.201706060
- URN
-
urn:nbn:de:101:1-2022091707155760546474
- Rights
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
- 15.08.2025, 7:34 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Zinke, Maximilian
- Fricke, Pascal
- Samson, Camille
- Hwang, Songhwan
- Wall, Joseph S.
- Lange, Sascha
- Zinn‐Justin, Sophie
- Lange, Adam
Other Objects (12)
Bacteriophage Tail‐Tube Assembly Studied by Proton‐Detected 4D Solid‐State NMR
Dual function of a highly conserved bacteriophage tail completion protein essential for bacteriophage infectivity
Architecture of the flexible tail tube of bacteriophage SPP1
Nearly complete structure of bacteriophage DT57C reveals architecture of head-to-tail interface and lateral tail fibers
Structural mechanism of bacteriophage lambda tail’s interaction with the bacterial receptor
Self-assembly of transmembrane peptides studied by solid-state NMR
Interactions of bacteriophage T4 adhesin with selected lipopolysaccharides studied using atomic force microscopy
Interactions of bacteriophage T4 adhesin with selected lipopolysaccharides studied using atomic force microscopy
Investigation of the tail tube protein gp17.1 by solid-state NMR
High-resolution reconstruction of a Jumbo-bacteriophage infecting capsulated bacteria using hyperbranched tail fibers
Simultaneous display of two large proteins on the head and tail of bacteriophage lambda
Characterization and genome annotation of a newly detected bacteriophage infecting multidrug-resistant Acinetobacter baumannii
Bacteriophage Tail‐Tube Assembly Studied by Proton‐Detected 4D Solid‐State NMR
Dual function of a highly conserved bacteriophage tail completion protein essential for bacteriophage infectivity
Architecture of the flexible tail tube of bacteriophage SPP1
Nearly complete structure of bacteriophage DT57C reveals architecture of head-to-tail interface and lateral tail fibers
Structural mechanism of bacteriophage lambda tail’s interaction with the bacterial receptor
Self-assembly of transmembrane peptides studied by solid-state NMR
Interactions of bacteriophage T4 adhesin with selected lipopolysaccharides studied using atomic force microscopy
Interactions of bacteriophage T4 adhesin with selected lipopolysaccharides studied using atomic force microscopy
Investigation of the tail tube protein gp17.1 by solid-state NMR
High-resolution reconstruction of a Jumbo-bacteriophage infecting capsulated bacteria using hyperbranched tail fibers
Simultaneous display of two large proteins on the head and tail of bacteriophage lambda
Characterization and genome annotation of a newly detected bacteriophage infecting multidrug-resistant Acinetobacter baumannii
Bacteriophage Tail‐Tube Assembly Studied by Proton‐Detected 4D Solid‐State NMR
Dual function of a highly conserved bacteriophage tail completion protein essential for bacteriophage infectivity
Architecture of the flexible tail tube of bacteriophage SPP1
Nearly complete structure of bacteriophage DT57C reveals architecture of head-to-tail interface and lateral tail fibers
Structural mechanism of bacteriophage lambda tail’s interaction with the bacterial receptor
Self-assembly of transmembrane peptides studied by solid-state NMR
Interactions of bacteriophage T4 adhesin with selected lipopolysaccharides studied using atomic force microscopy
Interactions of bacteriophage T4 adhesin with selected lipopolysaccharides studied using atomic force microscopy
Investigation of the tail tube protein gp17.1 by solid-state NMR
High-resolution reconstruction of a Jumbo-bacteriophage infecting capsulated bacteria using hyperbranched tail fibers
Simultaneous display of two large proteins on the head and tail of bacteriophage lambda