title: Site-specific solid-state NMR studies of "trigger factor" in complex with the large ribosomal subunit 50S.
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.
authors: Department Chemie, Technische Universität München, Lichtenbergstrasse 4, 85747, Garching (Germany).
authors: Emeline
authors: E
authors: Barbet-Massin
authors: Chih-Ting
authors: CT
authors: Huang
authors: Venita
authors: V
authors: Daebel
authors: Shang-Te Danny
authors: ST
authors: Hsu
authors: Bernd
authors: B
authors: Reif
mesh_terms: D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D017510:Protein Folding; D012270:Ribosomes / Q000737:chemistry*
keywords: NMR spectroscopy; magic-angle spinning (MAS); protein-protein interactions; ribosome complex; trigger factor