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Site‐Specific Solid‐State NMR Studies of “Trigger Factor” in Complex with the Large Ribosomal Subunit 50S
Author(s) -
BarbetMassin Emeline,
Huang ChihTing,
Daebel Venita,
Hsu ShangTe Danny,
Reif Bernd
Publication year - 2015
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201409393
Subject(s) - ribosome , 50s , ribosomal protein , chemistry , translation (biology) , ribosomal rna , crystallography , nuclear magnetic resonance spectroscopy , biophysics , solid state nuclear magnetic resonance , folding (dsp implementation) , chemical shift , nuclear magnetic resonance , stereochemistry , biology , biochemistry , physics , rna , messenger rna , electrical engineering , gene , engineering
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.