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Secondary structure from chemical shifts:
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From structure:
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From sequence:
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Disordered proteins:
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Format conversion & validation:
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From NMR-STAR 3.1
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Default Site-Specific Solid-State NMR Studies of "Trigger Factor" in Complex with the Large Ribosomal Subunit 50S.

Site-Specific Solid-State NMR Studies of "Trigger Factor" in Complex with the Large Ribosomal Subunit 50S.

Related Articles Site-Specific Solid-State NMR Studies of "Trigger Factor" in Complex with the Large Ribosomal Subunit 50S.

Angew Chem Int Ed Engl. 2015 Feb 5;

Authors: Barbet-Massin E, Huang CT, Daebel V, Hsu ST, Reif B

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.


PMID: 25655173 [PubMed - as supplied by publisher]



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