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- Title
Site-Specific Solid-State NMR Studies of 'Trigger Factor' in Complex with the Large Ribosomal Subunit 50S.
- Authors
Barbet-Massin, Emeline; Huang, Chih-Ting; Daebel, Venita; Hsu, Shang-Te Danny; Reif, Bernd
- Abstract
Co-translational protein folding is not yet well understood despite the availability of high-resolution ribosome crystal structures. We present first solid-state NMR data on non-mobile regions of a prokaryotic ribosomal complex. Localized chemical shift perturbations and line broadening are observed for the backbone amide resonances corresponding to the regions in the trigger factor ribosome-binding domain that are involved in direct contact with the ribosome or undergo conformational changes upon ribosome binding. This large asymmetric protein complex (1.4 MDa) becomes accessible for NMR investigations by the combined use of proton detection and high MAS frequencies (60 kHz). The presented results open new perspectives for the understanding of the mechanism of large molecular machineries.
- Subjects
NUCLEAR magnetic resonance; CRYSTAL structure; CHEMICAL shift (Nuclear magnetic resonance); X-ray crystallography; ELECTRON microscopy; MAGIC angle spinning
- Publication
Angewandte Chemie International Edition, 2015, Vol 54, Issue 14, p4367
- ISSN
1433-7851
- Publication type
Article
- DOI
10.1002/anie.201409393