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Protein folding on the ribosome studied using NMR spectroscopy.

Waudby, CA; Launay, H; Cabrita, LD; Christodoulou, J; (2013) Protein folding on the ribosome studied using NMR spectroscopy. Prog Nucl Magn Reson Spectrosc , 74 57 - 75. 10.1016/j.pnmrs.2013.07.003. Green open access

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Abstract

NMR spectroscopy is a powerful tool for the investigation of protein folding and misfolding, providing a characterization of molecular structure, dynamics and exchange processes, across a very wide range of timescales and with near atomic resolution. In recent years NMR methods have also been developed to study protein folding as it might occur within the cell, in a de novo manner, by observing the folding of nascent polypeptides in the process of emerging from the ribosome during synthesis. Despite the 2.3MDa molecular weight of the bacterial 70S ribosome, many nascent polypeptides, and some ribosomal proteins, have sufficient local flexibility that sharp resonances may be observed in solution-state NMR spectra. In providing information on dynamic regions of the structure, NMR spectroscopy is therefore highly complementary to alternative methods such as X-ray crystallography and cryo-electron microscopy, which have successfully characterized the rigid core of the ribosome particle. However, the low working concentrations and limited sample stability associated with ribosome-nascent chain complexes means that such studies still present significant technical challenges to the NMR spectroscopist. This review will discuss the progress that has been made in this area, surveying all NMR studies that have been published to date, and with a particular focus on strategies for improving experimental sensitivity.

Type: Article
Title: Protein folding on the ribosome studied using NMR spectroscopy.
Open access status: An open access version is available from UCL Discovery
DOI: 10.1016/j.pnmrs.2013.07.003
Publisher version: http://dx.doi.org/10.1016/j.pnmrs.2013.07.003
Additional information: �© 2013 Published by Elsevier B.V. This work is licensed under a Creative Commons Attribution 3.0 Unported License.
Keywords: Co-translational, Nuclear magnetic resonance, Protein folding, Ribosome, Sensitivity
UCL classification: UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Structural and Molecular Biology
URI: https://discovery.ucl.ac.uk/id/eprint/1425752
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