UCL Discovery
UCL home » Library Services » Electronic resources » UCL Discovery

The ribosome and its role in protein folding: looking through a magnifying glass

Javed, A; Christodoulou, J; Cabrita, LD; Orlova, EV; (2017) The ribosome and its role in protein folding: looking through a magnifying glass. Acta crystallographica. Section D, Structural biology , D73 pp. 509-521. 10.1107/S2059798317007446. Green open access

[thumbnail of id5003.pdf]
Preview
Text
id5003.pdf - Published Version

Download (2MB) | Preview

Abstract

Protein folding, a process that underpins cellular activity, begins co-translationally on the ribosome. During translation, a newly synthesized polypeptide chain enters the ribosomal exit tunnel and actively interacts with the ribosome elements – the r-proteins and rRNA that line the tunnel – prior to emerging into the cellular milieu. While understanding of the structure and function of the ribosome has advanced significantly, little is known about the process of folding of the emerging nascent chain (NC). Advances in cryo-electron microscopy are enabling visualization of NCs within the exit tunnel, allowing early glimpses of the interplay between the NC and the ribosome. Once it has emerged from the exit tunnel into the cytosol, the NC (still attached to its parent ribosome) can acquire a range of conformations, which can be characterized by NMR spectroscopy. Using experimental restraints within molecular-dynamics simulations, the ensemble of NC structures can be described. In order to delineate the process of co-translational protein folding, a hybrid structural biology approach is foreseeable, potentially offering a complete atomic description of protein folding as it occurs on the ribosome.

Type: Article
Title: The ribosome and its role in protein folding: looking through a magnifying glass
Open access status: An open access version is available from UCL Discovery
DOI: 10.1107/S2059798317007446
Publisher version: https://doi.org/10.1107/S2059798317007446
Language: English
Additional information: This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.
Keywords: Science & Technology, Life Sciences & Biomedicine, Physical Sciences, Biochemical Research Methods, Biochemistry & Molecular Biology, Biophysics, Crystallography, Ribosome, Nascent Chain, Protein Folding, NMR, Cryo-EM, Escherichia-Coli Ribosome, Nascent Polypeptide-Chains, Immune Electron-Microscopy, 5 S RNA, Angstrom Resolution, Messenger-Rna, Exit Tunnel, Structural Basis, 70S Ribosome, Mitochondrial Ribosome
UCL classification: UCL
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/1566672
Downloads since deposit
526Downloads
Download activity - last month
Download activity - last 12 months
Downloads by country - last 12 months

Archive Staff Only

View Item View Item